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2h2d

The Structural Basis for Sirtuin Substrate Affinity

Method: X-RAY DIFFRACTION Dmax: 64.5 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

NAD-dependent deacetylase

Thermotoga maritima

UniProt Q9WYW0

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–246 Fragment：Sir2Tm Cellular tumor antigen p53 peptide × 1 （P04637） ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 9.6；298 K；20% PEG 3350, 0.1 M CHES pH 9.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 9.60 Resolution 1.70 Å R-free 0.237

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 2H2D Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1YC5 Sir2-p53 peptide-nicotinamide Deposited 2004-12-21 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Not recorded ZN ZINC ION × 1 NCA NICOTINAMIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.6；293 K；CHES, PEG3350, nicotinamide, pH 9.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.40 Å R-free 0.202
2H2F The Structural basis for Sirtuin Substrate affinity Deposited 2006-05-18 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 9.6；298 K；20% PEG, pH 9.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 9.60
Resolution 2.20 Å R-free 0.246
2H2G The Structural Basis of Sirtuin substrate affinity Deposited 2006-05-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；293.15 K；20% PEG, pH 9.6, VAPOR DIFFUSION, HANGING DROP, pH 7.5, temperature 293.15K
Resolution 1.63 Å R-free 0.226
2H2G The Structural Basis of Sirtuin substrate affinity Deposited 2006-05-18 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；293.15 K；20% PEG, pH 9.6, VAPOR DIFFUSION, HANGING DROP, pH 7.5, temperature 293.15K
Resolution 1.63 Å R-free 0.226
2H2H The Structural basis of sirtuin substrate specificity Deposited 2006-05-18 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.5；293.15 K；20 % PEG, VAPOR DIFFUSION, HANGING DROP, temperature 293.15K, pH 9.5
Resolution 2.20 Å R-free 0.239
2H2I The Structural basis of Sirtuin Substrate Affinity Deposited 2006-05-18 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 8 PDB declaration: octameric
Chain A 1–246（246 aa）
Not recorded ZN ZINC ION × 8 ZPG (2S,5R,8R,11S,14S,17S,21R)-5,8,11,14,17-PENTAMETHYL-4,7,10,13,16,19-HEXAOXADOCOSANE-2,21-DIOL × 8 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.5M (NH4)2SO4, 4% PPG, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.80 Å R-free 0.213
2H4F Sir2-p53 peptide-NAD+ Deposited 2006-05-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Not recorded ZN ZINC ION × 1 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.6；293 K；CHES, PEG3350, NAD, pH 9.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.00 Å R-free 0.228
2H4H Sir2 H116Y mutant-p53 peptide-NAD Deposited 2006-05-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Mutation：H116Y ZN ZINC ION × 1 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.6；293 K；CHES, PEG 3350, pH9.6, NAD, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.99 Å R-free 0.237
2H4J Sir2-deacetylated peptide (from enzymatic turnover in crystal) Deposited 2006-05-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Not recorded ZN ZINC ION × 1 NCA NICOTINAMIDE × 1 OAD 2'-O-ACETYL ADENOSINE-5-DIPHOSPHORIBOSE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.6；293 K；CHES, PEG3350, PH9.6, acetylated peptide. Crystals were soaked in cryo + 5mM NAD, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.10 Å R-free 0.246
2H59 Sir2 H116A-deacetylated p53 peptide-3'-o-acetyl ADP ribose Deposited 2006-05-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 1–246（246 aa）
Chain B 1–246（246 aa）
Mutation：H116A Mutation：H116A ZN ZINC ION × 2 APR ADENOSINE-5-DIPHOSPHORIBOSE × 1 3OD (2S,3S,4R,5S)-2-({[(S)-{[(S)-{[(2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3,4-DIHYDROXYTETRAHYDROFURAN-2-YL]METHOXY}(HYDROXY)PHOSPHORYL]OXY}(HYDROXY)PHOSPHORYL]OXY}METHYL)-4,5-DIHYDROXYTETRAHYDROFURAN-3-YL ACETATE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.2；PEG 8000, Na-Tartrate:K-Phosphate, NaCl, NAD, pH 5.2, VAPOR DIFFUSION, HANGING DROP, temperature 100K
Resolution 1.90 Å R-free 0.247
3D4B Crystal structure of Sir2Tm in complex with Acetyl p53 peptide and DADMe-NAD+ Deposited 2008-05-14 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Not recorded ZN ZINC ION × 1 DZD 5'-O-[(R)-{[(R)-{[(3R,4R)-1-(3-carbamoylbenzyl)-4-hydroxypyrrolidin-3-yl]methoxy}(hydroxy)phosphoryl]methyl}(hydroxy)phosphoryl]adenosine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.5；292 K；PEG 3350, pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K
Resolution 1.90 Å R-free 0.229
3D81 Sir2-S-alkylamidate complex crystal structure Deposited 2008-05-22 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.5；293 K；PEG3350, pH 9.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.50 Å R-free 0.246
3JR3 Sir2 bound to acetylated peptide Deposited 2009-09-08 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Mutation：H116A ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.2；298 K；pH 9.2, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 1.50 Å R-free 0.228
3PDH Structure of Sir2Tm bound to a propionylated peptide Deposited 2010-10-22 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；Crystals were obtained from 1:1 mix of protein and the well solution (9.5% (w/v) PEG3350, 100 mM CHES buffer), pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.80 Å R-free 0.210
4BUZ SIR2 COMPLEX STRUCTURE MIXTURE OF EX-527 INHIBITOR AND REACTION PRODUCTS OR OF REACTION SUBSTRATES P53 PEPTIDE AND NAD Deposited 2013-06-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Not recorded OCZ (1S)-6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1- carboxamide × 1 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 OAD 2'-O-ACETYL ADENOSINE-5-DIPHOSPHORIBOSE × 1 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；8.5
Resolution 1.90 Å R-free 0.194
4BV2 CRYSTAL STRUCTURE OF SIR2 IN COMPLEX WITH THE INHIBITOR EX-527, 2'-O-ACETYL-ADP-RIBOSE AND DEACETYLATED P53-PEPTIDE Deposited 2013-06-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–246（246 aa）
Not recorded ZN ZINC ION × 1 OCZ (1S)-6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1- carboxamide × 1 OAD 2'-O-ACETYL ADENOSINE-5-DIPHOSPHORIBOSE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.9；20% PEG 6000, 0.1 M BIS-TRIS PH5.9
Resolution 3.30 Å R-free 0.318
4BV2 CRYSTAL STRUCTURE OF SIR2 IN COMPLEX WITH THE INHIBITOR EX-527, 2'-O-ACETYL-ADP-RIBOSE AND DEACETYLATED P53-PEPTIDE Deposited 2013-06-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 1–246（246 aa）
Not recorded ZN ZINC ION × 1 OCZ (1S)-6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1- carboxamide × 1 OAD 2'-O-ACETYL ADENOSINE-5-DIPHOSPHORIBOSE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.9；20% PEG 6000, 0.1 M BIS-TRIS PH5.9
Resolution 3.30 Å R-free 0.318
4BV2 CRYSTAL STRUCTURE OF SIR2 IN COMPLEX WITH THE INHIBITOR EX-527, 2'-O-ACETYL-ADP-RIBOSE AND DEACETYLATED P53-PEPTIDE Deposited 2013-06-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–246（246 aa）
Not recorded ZN ZINC ION × 1 OCZ (1S)-6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1- carboxamide × 1 OAD 2'-O-ACETYL ADENOSINE-5-DIPHOSPHORIBOSE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.9；20% PEG 6000, 0.1 M BIS-TRIS PH5.9
Resolution 3.30 Å R-free 0.318
4BV2 CRYSTAL STRUCTURE OF SIR2 IN COMPLEX WITH THE INHIBITOR EX-527, 2'-O-ACETYL-ADP-RIBOSE AND DEACETYLATED P53-PEPTIDE Deposited 2013-06-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 1–246（246 aa）
Not recorded ZN ZINC ION × 1 OCZ (1S)-6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1- carboxamide × 1 OAD 2'-O-ACETYL ADENOSINE-5-DIPHOSPHORIBOSE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.9；20% PEG 6000, 0.1 M BIS-TRIS PH5.9
Resolution 3.30 Å R-free 0.318

15 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NPD_THEMA
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–246； UniProt 1–246

Cellular tumor antigen p53 peptide

OrganismNot specified

UniProt P04637

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain B； UniProt 372–389 Non-standard monomer：Yes (specific site not provided by mmCIF) NAD-dependent deacetylase × 1 （Q9WYW0） ZN ZINC ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions：pH 9.6；298 K；20% PEG 3350, 0.1 M CHES pH 9.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 9.60 Resolution 1.70 Å R-free 0.237

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB Difference from Current Entry 2H2D Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1A1U SOLUTION STRUCTURE DETERMINATION OF A P53 MUTANT DIMERIZATION DOMAIN, NMR, MINIMIZED AVERAGE STRUCTURE Deposited 1997-12-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 324–358（35 aa） Fragment：OLIGOMERIZATION
Chain C 324–358（35 aa） Fragment：OLIGOMERIZATION
Mutation：M40K, F41I, L44Y Mutation：M40K, F41I, L44Y No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；313 K
Resolution not provided
1AIE P53 TETRAMERIZATION DOMAIN CRYSTAL STRUCTURE Deposited 1997-04-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 326–356（31 aa） Fragment：TETRAMERIZATION DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 8；1.4 M SODIUM CITRATE, 100 MM HEPES, PH 8.0
Resolution 1.50 Å R-free 0.252
1C26 CRYSTAL STRUCTURE OF P53 TETRAMERIZATION DOMAIN Deposited 1999-07-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 325–356（32 aa） Fragment：TETRAMERIZATION DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.8；298 K；3.0 M SODIUM FORMATE 0.5 M AMMONIUM SULFATE 50 MM TRIS-HCL PH 8.8, VAPOR DIFFUSION, HANGING DROP at 298 K
Resolution 1.70 Å
1DT7 SOLUTION STRUCTURE OF THE C-TERMINAL NEGATIVE REGULATORY DOMAIN OF P53 IN A COMPLEX WITH CA2+-BOUND S100B(BB) Deposited 2000-01-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain X 367–388（22 aa） Fragment：C-TERMINAL PEPTIDE
Chain Y 367–388（22 aa） Fragment：C-TERMINAL PEPTIDE
Not recorded CA CALCIUM ION × 4 SOLUTION NMR
NMR measurement conditions pH 6.5；310 K；Ionic strength (raw mmCIF value) 25 mM；Pressure ambient
NMR sample composition 3-6 mM S100 (subunit concentration), 0.1 mM EDTA, 0.34 mM NaN3, 5 mM DTT, 17 mM NaCl, 10 mM d11-tris-HCl, 7% D2O, 6-13 mM CaCl2, 4.8-10 mM p53 peptide | 7% D2O, 93% H2O
Resolution not provided
1GZH Crystal structure of the BRCT domains of human 53BP1 bound to the p53 tumor supressor Deposited 2002-05-22 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 95–292（198 aa） Fragment：DNA BINDING REGION, RESIDUES 95-292
Not recorded ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.4；50 MM TRIS PH 7.4, 250 MM AMMONIUM SULFATE, 25% POLYETHYLENE GLYCOL 4000
Resolution 2.60 Å R-free 0.288
1GZH Crystal structure of the BRCT domains of human 53BP1 bound to the p53 tumor supressor Deposited 2002-05-22 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 95–292（198 aa） Fragment：DNA BINDING REGION, RESIDUES 95-292
Not recorded ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.4；50 MM TRIS PH 7.4, 250 MM AMMONIUM SULFATE, 25% POLYETHYLENE GLYCOL 4000
Resolution 2.60 Å R-free 0.288
1H26 CDK2/CyclinA in complex with an 11-residue recruitment peptide from p53 Deposited 2002-07-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain E 376–386（11 aa） Fragment：RESIDUES 376-386
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；0.8M KCL, 1.2M (NH4)2SO4, 40MM HEPES PH 7.0. PROTEIN CONCENTRATION = 10MG/ML
Resolution 2.24 Å R-free 0.268
1HS5 NMR SOLUTION STRUCTURE OF DESIGNED P53 DIMER Deposited 2000-12-22 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 324–357（34 aa） Fragment：RESIDUES 324-357
Chain B 324–357（34 aa） Fragment：RESIDUES 324-357
Mutation：M340Q, L344R Mutation：M340Q, L344R No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；300 K；Ionic strength (raw mmCIF value) 25mM；Pressure ambient
NMR sample composition 2mM U-15N,13C; 25mM sodium phosphate; 150mM sodium chloride | 90% H2O/10% D2O
Resolution not provided
1JSP NMR Structure of CBP Bromodomain in complex with p53 peptide Deposited 2001-08-17 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 367–386（20 aa） Fragment：C-terminal fragment
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Pressure ambient
NMR measurement conditions pH 6.5；298 K；Pressure ambient
NMR measurement conditions pH 6.5；298 K；Pressure ambient
NMR measurement conditions pH 6.5；298 K；Pressure ambient
NMR sample composition 0.5mM CBP bromodomain U-15N; 0.5mM P53 peptide; 100mM phosphate buffer; pH 6.5 | 90% H2O/10% D2O
NMR sample composition 0.5mM CBP bromodomain U-15N,13C; 0.5mM P53 peptide;100mM phosphate buffer; pH 6.5 | 90% H2O/10% D2O
NMR sample composition 0.5mM CBP bromodomain U-15N,13C; 0.5mM P53 peptide;100mM phosphate buffer; pH 6.5 | 99.9%D2O
NMR sample composition 0.5mM CBP bromodomain U-15N,13C,75% 2H; 0.5mM P53 peptide;100mM phosphate buffer; pH 6.5 | 90% H2O/10% D2O
Resolution not provided
1KZY Crystal Structure of the 53bp1 BRCT Region Complexed to Tumor Suppressor P53 Deposited 2002-02-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 95–289（195 aa） Fragment：DNA-BINDING CORE DOMAIN
Chain B 95–289（195 aa） Fragment：DNA-BINDING CORE DOMAIN
Not recorded ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；277 K；PEG4000, sodium citrate, ammonium acetate, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.50 Å R-free 0.256
1MA3 Structure of a Sir2 enzyme bound to an acetylated p53 peptide Deposited 2002-07-31 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 372–389（18 aa） Fragment：Regulatory C-terminal tail (residues 372-389)
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 5.5；291 K；PEG 8000, PEG 1000 and Sodium Chloride, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 2.00 Å R-free 0.254
1OLG HIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR Deposited 1994-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 319–360（42 aa）
Chain B 319–360（42 aa）
Chain C 319–360（42 aa）
Chain D 319–360（42 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1OLH HIGH-RESOLUTION SOLUTION STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR Deposited 1994-06-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 319–360（42 aa）
Chain B 319–360（42 aa）
Chain C 319–360（42 aa）
Chain D 319–360（42 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1PES NMR SOLUTION STRUCTURE OF THE TETRAMERIC MINIMUM TRANSFORMING DOMAIN OF P53 Deposited 1994-11-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 325–355（31 aa）
Chain B 325–355（31 aa）
Chain C 325–355（31 aa）
Chain D 325–355（31 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1PET NMR SOLUTION STRUCTURE OF THE TETRAMERIC MINIMUM TRANSFORMING DOMAIN OF P53 Deposited 1994-11-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 325–355（31 aa）
Chain B 325–355（31 aa）
Chain C 325–355（31 aa）
Chain D 325–355（31 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1SAE HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR (SAC STRUCTURES) Deposited 1995-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 319–360（42 aa）
Chain B 319–360（42 aa）
Chain C 319–360（42 aa）
Chain D 319–360（42 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1SAF HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR (SAD STRUCTURES) Deposited 1995-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 319–360（42 aa）
Chain B 319–360（42 aa）
Chain C 319–360（42 aa）
Chain D 319–360（42 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1SAK HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR (SAC STRUCTURES) Deposited 1995-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 319–360（42 aa）
Chain B 319–360（42 aa）
Chain C 319–360（42 aa）
Chain D 319–360（42 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1SAL HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR (SAD STRUCTURES) Deposited 1995-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 319–360（42 aa）
Chain B 319–360（42 aa）
Chain C 319–360（42 aa）
Chain D 319–360（42 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1TSR P53 CORE DOMAIN IN COMPLEX WITH DNA Deposited 1995-07-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 3 PDB declaration: pentameric
Chain A 94–312（219 aa）
Chain B 94–312（219 aa）
Chain C 94–312（219 aa）
Not recorded ZN ZINC ION × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å
1TUP TUMOR SUPPRESSOR P53 COMPLEXED WITH DNA Deposited 1995-07-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 3 PDB declaration: pentameric
Chain A 94–312（219 aa）
Chain B 94–312（219 aa）
Chain C 94–312（219 aa）
Not recorded ZN ZINC ION × 3 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å
1UOL Crystal structure of the human p53 core domain mutant M133L/V203A/N239Y/N268D at 1.9 A resolution. Deposited 2003-09-19 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA BINDING (CORE) DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.2；pH 7.20
Resolution 1.90 Å R-free 0.230
1UOL Crystal structure of the human p53 core domain mutant M133L/V203A/N239Y/N268D at 1.9 A resolution. Deposited 2003-09-19 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA BINDING (CORE) DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.2；pH 7.20
Resolution 1.90 Å R-free 0.230
1XQH Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH Deposited 2004-10-12 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 369–377（9 aa） Fragment：mono-methylated p53 peptide
Non-standard monomer：Yes (specific site not provided by mmCIF) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.8；291 K；PEG3350, Tris-HCL, pH 7.8, VAPOR DIFFUSION, temperature 291K
Resolution 1.75 Å R-free 0.223
1XQH Crystal structure of a ternary complex of the methyltransferase SET9 (also known as SET7/9) with a P53 peptide and SAH Deposited 2004-10-12 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 369–377（9 aa） Fragment：mono-methylated p53 peptide
Non-standard monomer：Yes (specific site not provided by mmCIF) SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.8；291 K；PEG3350, Tris-HCL, pH 7.8, VAPOR DIFFUSION, temperature 291K
Resolution 1.75 Å R-free 0.223
1YCQ XENOPUS LAEVIS MDM2 BOUND TO THE TRANSACTIVATION DOMAIN OF HUMAN P53 Deposited 1996-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain B 13–29（17 aa） Fragment：RESIDUES 13 - 29
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.30 Å R-free 0.253
1YCR MDM2 BOUND TO THE TRANSACTIVATION DOMAIN OF P53 Deposited 1996-09-30 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 15–29（15 aa） Fragment：RESIDUES 15 - 29
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.60 Å R-free 0.276
1YCS P53-53BP2 COMPLEX Deposited 1996-09-30 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 94–292（199 aa） Fragment：RESIDUES 97 - 287
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.20 Å R-free 0.286
2AC0 Structural Basis of DNA Recognition by p53 Tetramers (complex I) Deposited 2005-07-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 94–293（200 aa） Fragment：residues 94-293
Chain B 94–293（200 aa） Fragment：residues 94-293
Chain C 94–293（200 aa） Fragment：residues 94-293
Chain D 94–293（200 aa） Fragment：residues 94-293
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；293 K；Ammonium Formate, PEG 3350, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.80 Å R-free 0.217
2ADY Structural Basis of DNA Recognition by p53 Tetramers (complex IV) Deposited 2005-07-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 94–293（200 aa） Fragment：residues 94-293
Chain B 94–293（200 aa） Fragment：residues 94-293
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.2；293 K；Ammonium Fluoride, PEG 3350, pH 6.2, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.50 Å R-free 0.251
2AHI Structural Basis of DNA Recognition by p53 Tetramers (complex III) Deposited 2005-07-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 94–293（200 aa） Fragment：residues 94-293
Chain B 94–293（200 aa） Fragment：residues 94-293
Chain C 94–293（200 aa） Fragment：residues 94-293
Chain D 94–293（200 aa） Fragment：residues 94-293
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.3；293 K；Ammonium Chloride, PEG 3350, pH 6.3, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.85 Å R-free 0.225
2ATA Structural Basis of DNA Recognition by p53 Tetramers (complex II) Deposited 2005-08-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 94–293（200 aa） Fragment：residues 94-293
Chain B 94–293（200 aa） Fragment：residues 94-293
Chain C 94–293（200 aa） Fragment：residues 94-293
Chain D 94–293（200 aa） Fragment：residues 94-293
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.7；293 K；Lithium Chloride, PEG 3350, pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.20 Å R-free 0.215
2B3G p53N (fragment 33-60) bound to RPA70N Deposited 2005-09-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain B 33–60（28 aa） Fragment：residues 33-60
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.9；298 K；Na3 Citrate, Hepes, pH 7.9, VAPOR DIFFUSION, SITTING DROP, temperature 298K, pH 7.90
Resolution 1.60 Å R-free 0.239
2BIM human p53 core domain mutant M133L-V203A-N239Y-N268D-R273H Deposited 2005-01-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING (CORE) DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.98 Å R-free 0.223
2BIM human p53 core domain mutant M133L-V203A-N239Y-N268D-R273H Deposited 2005-01-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING (CORE) DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.98 Å R-free 0.223
2BIN human p53 core domain mutant M133L-H168R-V203A-N239Y-N268D Deposited 2005-01-25 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING (CORE) DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.90 Å R-free 0.236
2BIO human p53 core domain mutant M133L-V203A-N239Y-R249S-N268D Deposited 2005-01-25 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING (CORE) DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.90 Å R-free 0.234
2BIP human p53 core domain mutant M133L-H168R-V203A-N239Y-R249S-N268D Deposited 2005-01-25 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING (CORE) DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å R-free 0.235
2BIQ human p53 core domain mutant T123A-M133L-H168R-V203A-N239Y-R249S- N268D Deposited 2005-01-25 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING (CORE) DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å R-free 0.255
2F1X Crystal structure of the TRAF-like domain of HAUSP/USP7 bound to a p53 peptide Deposited 2005-11-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 360–368（9 aa） Fragment：p53 peptide fusion with HAUSP N terminal
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG2000 monomethylether, calcium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.30 Å R-free 0.263
2F1X Crystal structure of the TRAF-like domain of HAUSP/USP7 bound to a p53 peptide Deposited 2005-11-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain B 360–368（9 aa） Fragment：p53 peptide fusion with HAUSP N terminal
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG2000 monomethylether, calcium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.30 Å R-free 0.263
2GS0 NMR structure of the complex between the PH domain of the Tfb1 subunit from TFIIH and the activation domain of p53 Deposited 2006-04-25 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 20–73（54 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；300 K；Ionic strength (raw mmCIF value) 20 mM sodium phosphate；Pressure ambient
NMR sample composition 1.0 mM Tfb1 U-15N, 1.0 mM p53 unlabeled, 1.00 mM EDTA, 20 mM phosphate buffer; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 1.0 mM Tfb1 U-15N,13C, 1.0 mM p53 unlabeled, 1.00 mM EDTA, 20 mM phosphate buffer; 100% D20 | 100% D20
NMR sample composition 1.0 mM p53 U-15N, 1.0 mM Tfb1 unlabeled, 1.00 mM EDTA, 20 mM phosphate buffer; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 1.0 mM p53 U-15N, 1.0 mM Tfb1 unlabeled, 1.00 mM EDTA, 20 mM phosphate buffer; 100% D20 | 100% D20
Resolution not provided
2H2F The Structural basis for Sirtuin Substrate affinity Deposited 2006-05-18 Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 372–389（18 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 9.6；298 K；20% PEG, pH 9.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 9.60
Resolution 2.20 Å R-free 0.246
2H4J Sir2-deacetylated peptide (from enzymatic turnover in crystal) Deposited 2006-05-24 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 372–389（18 aa）
Not recorded ZN ZINC ION × 1 NCA NICOTINAMIDE × 1 OAD 2'-O-ACETYL ADENOSINE-5-DIPHOSPHORIBOSE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 9.6；293 K；CHES, PEG3350, PH9.6, acetylated peptide. Crystals were soaked in cryo + 5mM NAD, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.10 Å R-free 0.246
2J0Z p53 tetramerization domain wild type Deposited 2006-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 326–356（31 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 326-356
Chain B 326–356（31 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 326-356
Chain C 326–356（31 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 326-356
Chain D 326–356（31 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 326-356
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.2；300 K；Pressure 1.0
NMR sample composition 5% D2O/95% WATER
Resolution not provided
2J10 p53 tetramerization domain mutant T329F Q331K Deposited 2006-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 326–356（31 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 326-356
Chain B 326–356（31 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 326-356
Chain C 326–356（31 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 326-356
Chain D 326–356（31 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 326-356
Mutation：YES Mutation：YES Mutation：YES Mutation：YES No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.2；300 K；Pressure 1.0
NMR sample composition 5% D2O/95% WATER
Resolution not provided
2J11 p53 tetramerization domain mutant Y327S T329G Q331G Deposited 2006-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 326–356（31 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 326-356
Chain B 326–356（31 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 326-356
Chain C 326–356（31 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 326-356
Chain D 326–356（31 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 326-356
Mutation：YES Mutation：YES Mutation：YES Mutation：YES No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.2；300 K；Pressure 1.0
NMR sample composition 5% D2O/95% WATER
Resolution not provided
2J1W Human p53 core domain mutant M133L-V143A-V203A-N239Y-N268D Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å R-free 0.206
2J1W Human p53 core domain mutant M133L-V143A-V203A-N239Y-N268D Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å R-free 0.206
2J1X Human p53 core domain mutant M133L-V203A-Y220C-N239Y-N268D Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.65 Å R-free 0.206
2J1X Human p53 core domain mutant M133L-V203A-Y220C-N239Y-N268D Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.65 Å R-free 0.206
2J1Y Human p53 core domain mutant M133L-V203A-N239Y-G245S-N268D Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-293
Mutation：YES ZN ZINC ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.69 Å R-free 0.218
2J1Y Human p53 core domain mutant M133L-V203A-N239Y-G245S-N268D Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–293（200 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-293
Mutation：YES ZN ZINC ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.69 Å R-free 0.218
2J1Y Human p53 core domain mutant M133L-V203A-N239Y-G245S-N268D Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–293（200 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-293
Mutation：YES ZN ZINC ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.69 Å R-free 0.218
2J1Y Human p53 core domain mutant M133L-V203A-N239Y-G245S-N268D Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–293（200 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-293
Mutation：YES ZN ZINC ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.69 Å R-free 0.218
2J1Z Human p53 core domain mutant M133L-V203A-N239Y-N268D-F270L Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å R-free 0.213
2J1Z Human p53 core domain mutant M133L-V203A-N239Y-N268D-F270L Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å R-free 0.213
2J20 Human p53 core domain mutant M133L-V203A-N239Y-N268D-R273C Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å R-free 0.206
2J20 Human p53 core domain mutant M133L-V203A-N239Y-N268D-R273C Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.80 Å R-free 0.206
2J21 Human p53 core domain mutant M133L-V203A-N239Y-N268D-R282W Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.60 Å R-free 0.224
2J21 Human p53 core domain mutant M133L-V203A-N239Y-N268D-R282W Deposited 2006-08-15 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING CORE DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.60 Å R-free 0.224
2K8F Structural Basis for the Regulation of p53 Function by p300 Deposited 2008-09-08 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–39（39 aa） Fragment：UNP residues 1-39
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.3；308 K；Ionic strength (raw mmCIF value) 200；Pressure ambient
NMR sample composition 1.1 mM TAZ2, 1.0 mM [U-100% 15N] TAD(1-39), 1.0 mM [U-100% 13C; U-100% 15N] TAD(1-39), 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.0 mM [U-100% 15N] TAZ2, 1.1 mM TAD(1-39), 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.0 mM [U-100% 13C; U-100% 15N] TAZ2, 1.1 mM TAD(1-39), 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.0 mM TAZ2, 1.1 mM TAD(1-39), 100% D2O | 100% D2O
Resolution not provided
2L14 Structure of CBP nuclear coactivator binding domain in complex with p53 TAD Deposited 2010-07-22 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 13–61（49 aa） Fragment：p53 TAD
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient
NMR sample composition 0.5 mM [U-99% 15N] CBP nuclear coactivator binding domain, 0.5 mM [U-99% 15N] p53 TAD, 0.5 mM [U-99% 13C; U-99% 15N] CBP nuclear coactivator binding domain, 0.5 mM [U-99% 13C; U-99% 15N] p53 TAD, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2LY4 HMGB1-facilitated p53 DNA binding occurs via HMG-box/p53 transactivation domain interaction and is regulated by the acidic tail Deposited 2012-09-12 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 1–93（93 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0.01；Pressure ambient
NMR sample composition 10 mM sodium phosphate, 1 mM EDTA, 1 mM DTT, 0.5 mM PMSF, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2MEJ Solution Structure of the Complex Between BCL-xL and the p53 Core Domain determined with PRE restraints Deposited 2013-09-25 Different construct Different mutation/modification Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 96–312（217 aa） Fragment：UNP residues 96-312
Not recorded ZN ZINC ION × 1 SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 0.05；Pressure ambient
NMR sample composition 0.6 mM [U-98% 13C; U-98% 15N; U-98% 2H] p53, 93% H2O/7% D2O | 93% H2O/7% D2O
NMR sample composition 0.1 mM [U-98% 15N; U-98% 2H] BCL-xL, 0.1 mM p53, 93% H2O/7% D2O | 93% H2O/7% D2O
NMR sample composition 0.6 mM [U-98% 13C; U-98% 15N; U-98% 2H] p53, 0.65 mM BCL-xL, 93% H2O/7% D2O | 93% H2O/7% D2O
NMR sample composition 0.1 mM [U-98% 15N; U-98% 2H] p53, 0.1 mM BCL-xL_C151MTSL, 93% H2O/7% D2O | 93% H2O/7% D2O
NMR sample composition 0.1 mM [U-98% 15N; U-98% 2H] p53, 0.1 mM BCL-xL_C151MTSL, 93% H2O/7% D2O | 93% H2O/7% D2O
NMR sample composition 0.1 mM [U-98% 15N; U-98% 2H] p53, 0.1 mM BCL-xL_C151S_S122C MTSL, 93% H2O/7% D2O | 93% H2O/7% D2O
NMR sample composition 0.1 mM [U-98% 15N; U-98% 2H] p53, 0.1 mM BCL-xL_C151S_S122C MTSL, 93% H2O/7% D2O | 93% H2O/7% D2O
NMR sample composition 0.1 mM [U-98% 15N; U-98% 2H] p53, 0.1 mM BCL-xL_C151S_S2C MTSL, 93% H2O/7% D2O | 93% H2O/7% D2O
NMR sample composition 0.1 mM [U-98% 15N; U-98% 2H] p53, 0.1 mM BCL-xL_C151S_S2C MTSL, 93% H2O/7% D2O | 93% H2O/7% D2O
NMR sample composition 0.1 mM [U-98% 15N; U-98% 2H] BCL-xL, 0.1 mM Co_p53, 93% H2O/7% D2O | 93% H2O/7% D2O
Resolution not provided
2MWO Solution structure of 53BP1 tandem Tudor domains in complex with a p53K370me2 peptide Deposited 2014-11-15 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 363–377（15 aa） Fragment：DNA-binding repression region residues 363-377
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.5；298 K；Ionic strength (raw mmCIF value) 25；Pressure ambient
NMR sample composition 25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K370me2, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K370me2, 100% D2O | 100% D2O
NMR sample composition 25 mM sodium phosphate, 1.5 mM sodium azide, 5.0 mM 53BP1-Tudor, 2.0 mM [U-100% 13C; U-100% 15N] p53Kc370me2, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 25 mM sodium phosphate, 1.5 mM sodium azide, 5.0 mM 53BP1-Tudor, 2.0 mM [U-100% 13C; U-100% 15N] p53Kc370me2, 100% D2O | 100% D2O
NMR sample composition 25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 15N] 53BP1-Tudor, 6.0 mM p53K370me2, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 35 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM p53K370me2, 100% D2O | 100% D2O
NMR sample composition 25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] p53Kc370me2, 100% D2O | 100% D2O
Resolution not provided
2MWP Solution structure of 53BP1 tandem Tudor domains in complex with a p53K382me2 peptide Deposited 2014-11-15 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 376–387（12 aa） Fragment：DNA-binding repression region residues 376-387
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.5；298 K；Ionic strength (raw mmCIF value) 25；Pressure ambient
NMR sample composition 25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 13C; U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2, 100% D2O | 100% D2O
NMR sample composition 25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM 53BP1-Tudor, 0.5 mM [U-100% 13C; U-100% 15N] p53Kc382me2, 100% D2O | 100% D2O
NMR sample composition 25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM [U-100% 15N] 53BP1-Tudor, 6.0 mM p53K382me2, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 25 mM sodium phosphate, 1.5 mM sodium azide, 2.0 mM p53K382me2, 100% D2O | 100% D2O
NMR sample composition 25 mM sodium phosphate, 1.5 mM sodium azide, 0.5 mM [U-100% 13C; U-100% 15N] p53Kc382me2, 100% D2O | 100% D2O
Resolution not provided
2MWY Mdmx-p53 Deposited 2014-12-03 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 15–29（15 aa） Fragment：residues 15-23
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7；298 K；Ionic strength (raw mmCIF value) 200；Pressure ambient
NMR sample composition 1.0 mM [U-100% 13C; U-100% 15N] protein 1, 1.2 mM protein 2, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2MZD Characterization of the p300 Taz2-p53 TAD2 Complex and Comparison with the p300 Taz2-p53 TAD1 Complex Deposited 2015-02-11 Different construct Different mutation/modification Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 35–59（25 aa） Fragment：UNP residues 35-59
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.3；308 K；Ionic strength (raw mmCIF value) 200；Pressure ambient
NMR sample composition 1.1 mM Taz2 domain of Histone Acetyltransferase p300, 1.0 mM [U-100% 13C; U-100% 15N] TAD2 sub-domain of Cellular Tumor Antigen p53, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.0 mM [U-100% 15N] Taz2 domain of Histone Acetyltransferase p300, 1.1 mM TAD2 sub-domain of Cellular Tumor Antigen p53, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.0 mM [U-100% 13C; U-100% 15N] Taz2 domain of Histone Acetyltransferase p300, 1.1 mM TAD2 sub-domain of Cellular Tumor Antigen p53, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.0 mM Taz2 domain of Histone Acetyltransferase p300, 1.1 mM TAD2 sub-domain of Cellular Tumor Antigen p53, 100% D2O | 100% D2O
Resolution not provided
2OCJ Human p53 core domain in the absence of DNA Deposited 2006-12-20 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：core domain (residues 94-312)
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；293 K；2 ul protein solution (5 mg/ml protein in 20 mM Tris, pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 ul reservoir buffer consisting of 100 mM Hepes, pH 7.6, 10 mM DTT, and 14-21% (w/v) polyethylene glycol (PEG) 4000 above 500 ul reservoir buffer. Colorless plate-shaped crystals were obtained within a few days. VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.05 Å R-free 0.246
2OCJ Human p53 core domain in the absence of DNA Deposited 2006-12-20 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：core domain (residues 94-312)
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；293 K；2 ul protein solution (5 mg/ml protein in 20 mM Tris, pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 ul reservoir buffer consisting of 100 mM Hepes, pH 7.6, 10 mM DTT, and 14-21% (w/v) polyethylene glycol (PEG) 4000 above 500 ul reservoir buffer. Colorless plate-shaped crystals were obtained within a few days. VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.05 Å R-free 0.246
2OCJ Human p53 core domain in the absence of DNA Deposited 2006-12-20 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–312（219 aa） Fragment：core domain (residues 94-312)
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；293 K；2 ul protein solution (5 mg/ml protein in 20 mM Tris, pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 ul reservoir buffer consisting of 100 mM Hepes, pH 7.6, 10 mM DTT, and 14-21% (w/v) polyethylene glycol (PEG) 4000 above 500 ul reservoir buffer. Colorless plate-shaped crystals were obtained within a few days. VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.05 Å R-free 0.246
2OCJ Human p53 core domain in the absence of DNA Deposited 2006-12-20 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–312（219 aa） Fragment：core domain (residues 94-312)
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；293 K；2 ul protein solution (5 mg/ml protein in 20 mM Tris, pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 ul reservoir buffer consisting of 100 mM Hepes, pH 7.6, 10 mM DTT, and 14-21% (w/v) polyethylene glycol (PEG) 4000 above 500 ul reservoir buffer. Colorless plate-shaped crystals were obtained within a few days. VAPOR DIFFUSION, SITTING DROP, temperature 293K
Resolution 2.05 Å R-free 0.246
2PCX Crystal structure of p53DBD(R282Q) at 1.54-angstrom Resolution Deposited 2007-03-30 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–292（199 aa） Fragment：p53 DBD DOMAIN
Mutation：R282Q ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；300 K；0.1M ammonium acetate, 25% PEG 3350, 0.1M HEPES, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 300K
Resolution 1.54 Å R-free 0.232
2RUK Solution structure of the complex between p53 transactivation domain 2 and TFIIH p62 PH domain Deposited 2014-09-24 Different construct Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 41–62（22 aa） Fragment：p53 transactivation domain, UNP residues 41-62
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.8；305 K；Ionic strength (raw mmCIF value) 0.02；Pressure ambient
NMR sample composition 0.4 mM [U-99% 13C; U-99% 15N] TFIIH p62 PH domain-1, 0.48 mM p53 TAD2-2, 20 mM potassium phosphate-3, 5 mM [U-2H] DTT-4, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.4 mM [U-99% 13C; U-99% 15N] TFIIH p62 PH domain-5, 0.48 mM p53 TAD2-6, 20 mM potassium phosphate-7, 5 mM [U-2H] DTT-8, 100% D2O | 100% D2O
Resolution not provided
2VUK Structure of the p53 core domain mutant Y220C bound to the stabilizing small-molecule drug PhiKan083 Deposited 2008-05-26 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；294 K；SITTING DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES PH 7.2, 19 % PEG 4000, 5 MM DTT. CRYSTALS WERE SOAKED WITH 10 MM PHIKAN083 IN CRYO BUFFER CONTAINING 100 MM HEPES PH 7.2, 10 MM SODIUM PHOSPHATE PH 7.2, 19 % PEG 4000, 20 % GLYCEROL, 150 MM KCL.
Resolution 1.50 Å R-free 0.208
2VUK Structure of the p53 core domain mutant Y220C bound to the stabilizing small-molecule drug PhiKan083 Deposited 2008-05-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 P83 1-(9-ethyl-9H-carbazol-3-yl)-N-methylmethanamine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；294 K；SITTING DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES PH 7.2, 19 % PEG 4000, 5 MM DTT. CRYSTALS WERE SOAKED WITH 10 MM PHIKAN083 IN CRYO BUFFER CONTAINING 100 MM HEPES PH 7.2, 10 MM SODIUM PHOSPHATE PH 7.2, 19 % PEG 4000, 20 % GLYCEROL, 150 MM KCL.
Resolution 1.50 Å R-free 0.208
2WGX HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-Y236F-N239Y-T253I-N268D Deposited 2009-04-27 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；294 K；SITTING DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML IN 25 MM SODIUM PHOSPHATE PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES PH 7.2, 19 % PEG 4000, 5 MM DTT.
Resolution 1.75 Å R-free 0.199
2WGX HUMAN P53 CORE DOMAIN MUTANT M133L-V203A-Y236F-N239Y-T253I-N268D Deposited 2009-04-27 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；294 K；SITTING DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML IN 25 MM SODIUM PHOSPHATE PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES PH 7.2, 19 % PEG 4000, 5 MM DTT.
Resolution 1.75 Å R-free 0.199
2X0U STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO A 2-amino substituted benzothiazole scaffold Deposited 2009-12-17 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；294 K；SITTING DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES PH 7.2, 19% PEG 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF SMALL MOLECULE LIGAND IN 100 MM HEPES PH 7.2, 10 MM SODIUM PHOSPHATE PH 7.2, 19% PEG 4000, 20% GLYCEROL, 150 MM KCL.
Resolution 1.60 Å R-free 0.193
2X0U STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO A 2-amino substituted benzothiazole scaffold Deposited 2009-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X0U 6,7-DIHYDRO[1,4]DIOXINO[2,3-F][1,3]BENZOTHIAZOL-2-AMINE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；294 K；SITTING DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES PH 7.2, 19% PEG 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF SMALL MOLECULE LIGAND IN 100 MM HEPES PH 7.2, 10 MM SODIUM PHOSPHATE PH 7.2, 19% PEG 4000, 20% GLYCEROL, 150 MM KCL.
Resolution 1.60 Å R-free 0.193
2X0V STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO 4-(trifluoromethyl)benzene-1,2-diamine Deposited 2009-12-17 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；294 K；SITTING DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES PH 7.2, 19 % PEG 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF SMALL MOLECULE LIGAND IN 100 MM HEPES PH 7.2, 10 MM SODIUM PHOSPHATE PH 7.2, 19 % PEG 4000, 20 % GLYCEROL, 150 MM KCL.
Resolution 1.80 Å R-free 0.189
2X0V STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO 4-(trifluoromethyl)benzene-1,2-diamine Deposited 2009-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X0V 4-(TRIFLUOROMETHYL)BENZENE-1,2-DIAMINE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；294 K；SITTING DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES PH 7.2, 19 % PEG 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF SMALL MOLECULE LIGAND IN 100 MM HEPES PH 7.2, 10 MM SODIUM PHOSPHATE PH 7.2, 19 % PEG 4000, 20 % GLYCEROL, 150 MM KCL.
Resolution 1.80 Å R-free 0.189
2X0W STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO 5,6-dimethoxy- 2-methylbenzothiazole Deposited 2009-12-17 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES PH 7.2, 19% PEG 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF SMALL MOLECULE LIGAND IN 100 MM HEPES PH 7.2, 10 MM SODIUM PHOSPHATE PH 7.2, 19% PEG 4000, 20% GLYCEROL, 150 MM KCL.
Resolution 2.10 Å R-free 0.228
2X0W STRUCTURE OF THE P53 CORE DOMAIN MUTANT Y220C BOUND TO 5,6-dimethoxy- 2-methylbenzothiazole Deposited 2009-12-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X0W 5,6-DIMETHOXY-2-METHYL-1,3-BENZOTHIAZOLE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES PH 7.2, 19% PEG 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF SMALL MOLECULE LIGAND IN 100 MM HEPES PH 7.2, 10 MM SODIUM PHOSPHATE PH 7.2, 19% PEG 4000, 20% GLYCEROL, 150 MM KCL.
Resolution 2.10 Å R-free 0.228
2XWR Crystal structure of the DNA-binding domain of human p53 with extended N terminus Deposited 2010-11-04 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 89–293（205 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 89-293
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 5.4 MG/ML IN 25 MM SODIUM PHOSPHATE, PH 7.2, 220 MM NACL, AND 5 MM DTT. RESERVOIR SOLUTION: 100 MM BIS-TRIS, PH 5.5, 23% PEG 3350, 200 MM AMMONIUM SULFATE.
Resolution 1.68 Å R-free 0.209
2XWR Crystal structure of the DNA-binding domain of human p53 with extended N terminus Deposited 2010-11-04 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 89–293（205 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 89-293
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 5.4 MG/ML IN 25 MM SODIUM PHOSPHATE, PH 7.2, 220 MM NACL, AND 5 MM DTT. RESERVOIR SOLUTION: 100 MM BIS-TRIS, PH 5.5, 23% PEG 3350, 200 MM AMMONIUM SULFATE.
Resolution 1.68 Å R-free 0.209
2YBG Structure of Lys120-acetylated p53 core domain Deposited 2011-03-08 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-293
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions PROTEIN SOLUTION: 5 MG/ML PROTEIN IN 20 MM CITRATE BUFFER PH 6.1, 150 MM NACL, 10 MM DTT. CRYSTALLIZATION BUFFER: 26% (W/V) PEG 3350, 43 MM SODIUM ACETATE AND 100 MM HEPES, PH 7.5
Resolution 1.90 Å R-free 0.226
2YBG Structure of Lys120-acetylated p53 core domain Deposited 2011-03-08 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–293（200 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-293
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions PROTEIN SOLUTION: 5 MG/ML PROTEIN IN 20 MM CITRATE BUFFER PH 6.1, 150 MM NACL, 10 MM DTT. CRYSTALLIZATION BUFFER: 26% (W/V) PEG 3350, 43 MM SODIUM ACETATE AND 100 MM HEPES, PH 7.5
Resolution 1.90 Å R-free 0.226
2YBG Structure of Lys120-acetylated p53 core domain Deposited 2011-03-08 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–293（200 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-293
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions PROTEIN SOLUTION: 5 MG/ML PROTEIN IN 20 MM CITRATE BUFFER PH 6.1, 150 MM NACL, 10 MM DTT. CRYSTALLIZATION BUFFER: 26% (W/V) PEG 3350, 43 MM SODIUM ACETATE AND 100 MM HEPES, PH 7.5
Resolution 1.90 Å R-free 0.226
2YBG Structure of Lys120-acetylated p53 core domain Deposited 2011-03-08 Different construct Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–293（200 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-293
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions PROTEIN SOLUTION: 5 MG/ML PROTEIN IN 20 MM CITRATE BUFFER PH 6.1, 150 MM NACL, 10 MM DTT. CRYSTALLIZATION BUFFER: 26% (W/V) PEG 3350, 43 MM SODIUM ACETATE AND 100 MM HEPES, PH 7.5
Resolution 1.90 Å R-free 0.226
2YDR CpOGA D298N in complex with p53-derived O-GlcNAc peptide Deposited 2011-03-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain P 144–154（11 aa） Fragment：RESIDUES 144-154
Not recorded CD CADMIUM ION × 18 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；0.6 M NAAC, 0.175 M CDSO4, 0.1 M HEPES PH 7.5
Resolution 2.75 Å R-free 0.219
2Z5S Molecular basis for the inhibition of p53 by Mdmx Deposited 2007-07-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain P 15–29（15 aa） Fragment：TRANSACTIVATION DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；280 K；30% PEG 300, 0.1M MES pH6.5, VAPOR DIFFUSION, SITTING DROP, temperature 280K
Resolution 2.30 Å R-free 0.310
2Z5S Molecular basis for the inhibition of p53 by Mdmx Deposited 2007-07-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain Q 15–29（15 aa） Fragment：TRANSACTIVATION DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；280 K；30% PEG 300, 0.1M MES pH6.5, VAPOR DIFFUSION, SITTING DROP, temperature 280K
Resolution 2.30 Å R-free 0.310
2Z5S Molecular basis for the inhibition of p53 by Mdmx Deposited 2007-07-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain R 15–29（15 aa） Fragment：TRANSACTIVATION DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；280 K；30% PEG 300, 0.1M MES pH6.5, VAPOR DIFFUSION, SITTING DROP, temperature 280K
Resolution 2.30 Å R-free 0.310
2Z5T Molecular basis for the inhibition of p53 by Mdmx Deposited 2007-07-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain P 15–29（15 aa） Fragment：TRANSACTIVATION DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；280 K；30% PEG 300, 0.1M MES, pH6.5, VAPOR DIFFUSION, SITTING DROP, temperature 280K
Resolution 2.30 Å R-free 0.264
2Z5T Molecular basis for the inhibition of p53 by Mdmx Deposited 2007-07-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain Q 15–29（15 aa） Fragment：TRANSACTIVATION DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；280 K；30% PEG 300, 0.1M MES, pH6.5, VAPOR DIFFUSION, SITTING DROP, temperature 280K
Resolution 2.30 Å R-free 0.264
2Z5T Molecular basis for the inhibition of p53 by Mdmx Deposited 2007-07-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain R 15–29（15 aa） Fragment：TRANSACTIVATION DOMAIN
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；280 K；30% PEG 300, 0.1M MES, pH6.5, VAPOR DIFFUSION, SITTING DROP, temperature 280K
Resolution 2.30 Å R-free 0.264
3D05 Human p53 core domain with hot spot mutation R249S (II) Deposited 2008-05-01 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa） Fragment：p53 Core Domain, UNP residues 94-293
Mutation：R249S ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；0.2M Sodium Acetate, 20% PEG 3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.70 Å R-free 0.264
3D06 Human p53 core domain with hot spot mutation R249S (I) Deposited 2008-05-01 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa） Fragment：p53 Core Domain, UNP residues 94-293
Mutation：R249S ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；0.15M Sodium acetate, 20% PEG 3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.20 Å R-free 0.202
3D07 Human p53 core domain with hot spot mutation R249S (III) Deposited 2008-05-01 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa） Fragment：p53 Core Domain, UNP residues 94-293
Mutation：R249S ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；0.2M Sodium Acetate, 20% PEG 3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.20 Å R-free 0.256
3D07 Human p53 core domain with hot spot mutation R249S (III) Deposited 2008-05-01 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–293（200 aa） Fragment：p53 Core Domain, UNP residues 94-293
Mutation：R249S ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；0.2M Sodium Acetate, 20% PEG 3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.20 Å R-free 0.256
3D08 Human p53 core domain with hot spot mutation R249S and second-site suppressor mutation H168R Deposited 2008-05-01 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa） Fragment：p53 Core Domain, UNP residues 94-293
Mutation：R249S, H168R ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；0.2M Sodium acetate, 20% PEG3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.40 Å R-free 0.212
3D09 Human p53 core domain with hot spot mutation R249S and second-site suppressor mutations H168R and T123A Deposited 2008-05-01 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa） Fragment：p53 Core Domain, UNP residues 94-293
Mutation：R249S, H168R, T123A ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；0.2M Sodium Acetate, 20% PEG 3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.90 Å R-free 0.262
3D0A Human p53 core domain with hot spot mutation R249S and second site suppressor mutation H168R in sequence-specific complex with DNA Deposited 2008-05-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 94–293（200 aa） Fragment：P53 core domain, UNP residues 94-293
Chain B 94–293（200 aa） Fragment：P53 core domain, UNP residues 94-293
Mutation：R249S, H168R Mutation：R249S, H168R ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；0.2 M ammonium formate, 20% PEG 3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.80 Å R-free 0.241
3D0A Human p53 core domain with hot spot mutation R249S and second site suppressor mutation H168R in sequence-specific complex with DNA Deposited 2008-05-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain C 94–293（200 aa） Fragment：P53 core domain, UNP residues 94-293
Chain D 94–293（200 aa） Fragment：P53 core domain, UNP residues 94-293
Mutation：R249S, H168R Mutation：R249S, H168R ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；0.2 M ammonium formate, 20% PEG 3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.80 Å R-free 0.241
3DAB Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain Deposited 2008-05-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 15–29（15 aa） Fragment：UNP residues 15-29
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；300 K；25% PEG3350, 0.1M MES, pH6.5, VAPOR DIFFUSION, SITTING DROP, temperature 300K
Resolution 1.90 Å R-free 0.257
3DAB Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain Deposited 2008-05-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 15–29（15 aa） Fragment：UNP residues 15-29
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；300 K；25% PEG3350, 0.1M MES, pH6.5, VAPOR DIFFUSION, SITTING DROP, temperature 300K
Resolution 1.90 Å R-free 0.257
3DAB Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain Deposited 2008-05-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain F 15–29（15 aa） Fragment：UNP residues 15-29
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；300 K；25% PEG3350, 0.1M MES, pH6.5, VAPOR DIFFUSION, SITTING DROP, temperature 300K
Resolution 1.90 Å R-free 0.257
3DAB Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain Deposited 2008-05-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain H 15–29（15 aa） Fragment：UNP residues 15-29
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；300 K；25% PEG3350, 0.1M MES, pH6.5, VAPOR DIFFUSION, SITTING DROP, temperature 300K
Resolution 1.90 Å R-free 0.257
3DAC Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain Deposited 2008-05-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain P 17–37（21 aa） Fragment：UNP residues 17-37
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；300 K；30% PEG300, 0.1M MES, pH6.5, VAPOR DIFFUSION, SITTING DROP
Resolution 1.80 Å R-free 0.243
3DAC Structure of the human Mdmx protein bound to the p53 tumor suppressor transactivation domain Deposited 2008-05-29 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 17–37（21 aa） Fragment：UNP residues 17-37
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；300 K；30% PEG300, 0.1M MES, pH6.5, VAPOR DIFFUSION, SITTING DROP
Resolution 1.80 Å R-free 0.243
3IGK Diversity in DNA recognition by p53 revealed by crystal structures with Hoogsteen base pairs (p53-DNA complex 2) Deposited 2009-07-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 94–293（200 aa） Fragment：P53 core domain, unp residues 94-293
Mutation：H168R, R249S ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；0.16M SODIUM ACETATE, 16% PEG 3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.70 Å R-free 0.214
3IGL Diversity in DNA recognition by p53 revealed by crystal structures with Hoogsteen base pairs (p53-DNA complex 1) Deposited 2009-07-28 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 94–293（200 aa） Fragment：P53 core domain, unp residues 94-293
Not recorded ZN ZINC ION × 2 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；0.16M SODIUM ACETATE, 16% PEG 3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.80 Å R-free 0.212
3KMD Crystal structure of the p53 core domain bound to a full consensus site as a self-assembled tetramer Deposited 2009-11-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 92–291（200 aa） Fragment：UNP residues 92-291, DNA binding domain
Chain B 92–291（200 aa） Fragment：UNP residues 92-291, DNA binding domain
Chain C 92–291（200 aa） Fragment：UNP residues 92-291, DNA binding domain
Chain D 92–291（200 aa） Fragment：UNP residues 92-291, DNA binding domain
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions hanging drop；pH 6.68；291 K；16% PEG 4000, 142mM Nacl, pH 6.68, hanging drop, temperature 291K
Resolution 2.15 Å R-free 0.239
3KZ8 Diversity in DNA recognition by p53 revealed by crystal structures with Hoogsteen base pairs (p53-DNA complex 3) Deposited 2009-12-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 94–293（200 aa） Fragment：P53 core domain, UNP residues 94-293
Chain B 94–293（200 aa） Fragment：P53 core domain, UNP residues 94-293
Not recorded ZN ZINC ION × 4 IOD IODIDE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；0.20M AMMONIUM IODIDE, 20% PEG 3350, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.91 Å R-free 0.266
3LW1 Binary complex of 14-3-3 sigma and p53 pT387-peptide Deposited 2010-02-23 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 385–393（9 aa） Fragment：UNP residues 385-393
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 6 CL CHLORIDE ION × 2 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M HEPES, 0.2M calcium chloride, 28% PEG 400, 5% glycerol, 2mM DTT, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.28 Å R-free 0.151
3PDH Structure of Sir2Tm bound to a propionylated peptide Deposited 2010-10-22 Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 372–389（18 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；Crystals were obtained from 1:1 mix of protein and the well solution (9.5% (w/v) PEG3350, 100 mM CHES buffer), pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.80 Å R-free 0.210
3Q01 An induced fit mechanism regulates p53 DNA binding kinetics to confer sequence specificity Deposited 2010-12-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 94–291（198 aa） Fragment：p53 DNA-binding (Res 94-291) and Oligomerization (Res 322-356) domains
Chain A 322–356（35 aa） Fragment：p53 DNA-binding (Res 94-291) and Oligomerization (Res 322-356) domains
Chain B 94–291（198 aa） Fragment：p53 DNA-binding (Res 94-291) and Oligomerization (Res 322-356) domains
Chain B 322–356（35 aa） Fragment：p53 DNA-binding (Res 94-291) and Oligomerization (Res 322-356) domains
Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322T, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322T, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322T, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322T, L323M, M340Q, L344R, G356T ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.2M ammonium acetate, 0.1M HEPES, pH 7.5, 45% v/v 2-Methyl-2,4-pentanediol, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.10 Å R-free 0.282
3Q05 An induced fit mechanism regulates p53 DNA binding kinetics to confer sequence specificity Deposited 2010-12-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 94–291（198 aa） Fragment：p53 DNA-binding (Res 94-291) and Oligomerization (Res 321-356) domains
Chain A 321–356（36 aa） Fragment：p53 DNA-binding (Res 94-291) and Oligomerization (Res 321-356) domains
Chain B 94–291（198 aa） Fragment：p53 DNA-binding (Res 94-291) and Oligomerization (Res 321-356) domains
Chain B 321–356（36 aa） Fragment：p53 DNA-binding (Res 94-291) and Oligomerization (Res 321-356) domains
Chain C 94–291（198 aa） Fragment：p53 DNA-binding (Res 94-291) and Oligomerization (Res 321-356) domains
Chain C 321–356（36 aa） Fragment：p53 DNA-binding (Res 94-291) and Oligomerization (Res 321-356) domains
Chain D 94–291（198 aa） Fragment：p53 DNA-binding (Res 94-291) and Oligomerization (Res 321-356) domains
Chain D 321–356（36 aa） Fragment：p53 DNA-binding (Res 94-291) and Oligomerization (Res 321-356) domains
Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322A, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322A, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322A, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322A, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322A, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322A, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322A, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322A, L323M, M340Q, L344R, G356T ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；0.15M DL-Malic Acid [pH 7.0], 20% Polyethylene Glycol 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.40 Å R-free 0.267
3Q06 An induced fit mechanism regulates p53 DNA binding kinetics to confer sequence specificity Deposited 2010-12-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 96–292（197 aa） Fragment：p53 DNA-binding (Res 96-292) and Oligomerization (Res 321-356) domains
Chain A 321–354（34 aa） Fragment：p53 DNA-binding (Res 96-292) and Oligomerization (Res 321-356) domains
Chain B 96–292（197 aa） Fragment：p53 DNA-binding (Res 96-292) and Oligomerization (Res 321-356) domains
Chain B 321–354（34 aa） Fragment：p53 DNA-binding (Res 96-292) and Oligomerization (Res 321-356) domains
Chain C 96–292（197 aa） Fragment：p53 DNA-binding (Res 96-292) and Oligomerization (Res 321-356) domains
Chain C 321–354（34 aa） Fragment：p53 DNA-binding (Res 96-292) and Oligomerization (Res 321-356) domains
Chain D 96–292（197 aa） Fragment：p53 DNA-binding (Res 96-292) and Oligomerization (Res 321-356) domains
Chain D 321–354（34 aa） Fragment：p53 DNA-binding (Res 96-292) and Oligomerization (Res 321-356) domains
Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, M340Q, L344R, G356T ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；0.15M DL-Malic Acid pH 7.0, 20% Polyethylene Glycol 3350, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 3.20 Å R-free 0.314
3SAK HIGH RESOLUTION SOLUTION NMR STRUCTURE OF THE OLIGOMERIZATION DOMAIN OF P53 BY MULTI-DIMENSIONAL NMR (SAC STRUCTURES) Deposited 1999-04-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 319–360（42 aa） Fragment：OLIGOMERIZATION DOMAIN, RESIDUES 319 - 360
Chain B 319–360（42 aa） Fragment：OLIGOMERIZATION DOMAIN, RESIDUES 319 - 360
Chain C 319–360（42 aa） Fragment：OLIGOMERIZATION DOMAIN, RESIDUES 319 - 360
Chain D 319–360（42 aa） Fragment：OLIGOMERIZATION DOMAIN, RESIDUES 319 - 360
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions 308 K
Resolution not provided
3TG5 Structure of SMYD2 in complex with p53 and SAH Deposited 2011-08-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 365–375（11 aa） Fragment：UNP residues 365-375
Not recorded GOL GLYCEROL × 1 SAH S-ADENOSYL-L-HOMOCYSTEINE × 1 ZN ZINC ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；293 K；0.1M Hepes (pH 7.5), 25% PEG 3350, VAPOR DIFFUSION, temperature 293K
Resolution 2.30 Å R-free 0.263
3TS8 Crystal structure of a multidomain human p53 tetramer bound to the natural CDKN1A(p21) p53-response element Deposited 2011-09-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 94–291（198 aa） Fragment：p53 DNA-binding (UNP residues 94-291) and Oligomerization (UNP residues 321-356) domains
Chain A 321–356（36 aa） Fragment：p53 DNA-binding (UNP residues 94-291) and Oligomerization (UNP residues 321-356) domains
Chain B 94–291（198 aa） Fragment：p53 DNA-binding (UNP residues 94-291) and Oligomerization (UNP residues 321-356) domains
Chain B 321–356（36 aa） Fragment：p53 DNA-binding (UNP residues 94-291) and Oligomerization (UNP residues 321-356) domains
Chain C 94–291（198 aa） Fragment：p53 DNA-binding (UNP residues 94-291) and Oligomerization (UNP residues 321-356) domains
Chain C 321–356（36 aa） Fragment：p53 DNA-binding (UNP residues 94-291) and Oligomerization (UNP residues 321-356) domains
Chain D 94–291（198 aa） Fragment：p53 DNA-binding (UNP residues 94-291) and Oligomerization (UNP residues 321-356) domains
Chain D 321–356（36 aa） Fragment：p53 DNA-binding (UNP residues 94-291) and Oligomerization (UNP residues 321-356) domains
Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322t, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322t, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322t, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322t, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322t, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322t, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322t, L323M, M340Q, L344R, G356T Mutation：C135V, C141V, W146Y, C182S, V203A, R209P, C229Y, H233Y, Y234F, N235K, Y236F, T253V, N268D, P322t, L323M, M340Q, L344R, G356T ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；0.2 M potassium tartrate tetrahydrate, 20% Polyethylene Glycol 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.80 Å R-free 0.283
3ZME Structure of the p53 core domain mutant Y220C bound to the small molecule PhiKan7242 Deposited 2013-02-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：Y220C ZN ZINC ION × 1 QC5 2-(4-(4-fluorophenyl)-5-(1H-pyrrol-1-yl)-1H-pyrazol-1-yl)-N,N-dimethylethanamine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；294 K；CRYSTALLIZATION CONDITIONS: SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 40 MM COMPOUND (PK7204) IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL. SOAKING TIME: 3 HOURS.
Resolution 1.35 Å R-free 0.175
3ZME Structure of the p53 core domain mutant Y220C bound to the small molecule PhiKan7242 Deposited 2013-02-07 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：Y220C ZN ZINC ION × 1 QC5 2-(4-(4-fluorophenyl)-5-(1H-pyrrol-1-yl)-1H-pyrazol-1-yl)-N,N-dimethylethanamine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；294 K；CRYSTALLIZATION CONDITIONS: SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 40 MM COMPOUND (PK7204) IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL. SOAKING TIME: 3 HOURS.
Resolution 1.35 Å R-free 0.175
4AGL Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan784 Deposited 2012-01-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES P84 2,4-BIS(IODANYL)-6-[[METHYL-(1-METHYLPIPERIDIN-4-YL)AMINO]METHYL]PHENOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.70 Å R-free 0.193
4AGL Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan784 Deposited 2012-01-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES P84 2,4-BIS(IODANYL)-6-[[METHYL-(1-METHYLPIPERIDIN-4-YL)AMINO]METHYL]PHENOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.70 Å R-free 0.193
4AGM Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan5086 Deposited 2012-01-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES P86 2-{[4-(DIETHYLAMINO)PIPERIDIN-1-YL]METHYL}-4,6-DIIODOPHENOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.52 Å R-free 0.197
4AGM Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan5086 Deposited 2012-01-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES P86 2-{[4-(DIETHYLAMINO)PIPERIDIN-1-YL]METHYL}-4,6-DIIODOPHENOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.52 Å R-free 0.197
4AGN Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan5116 Deposited 2012-01-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 NXG 2-{[4-(DIETHYLAMINO)PIPERIDIN-1-YL]METHYL}-4-(3-HYDROXYPROP-1-YN-1-YL)-6-IODOPHENOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.60 Å R-free 0.194
4AGN Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan5116 Deposited 2012-01-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 NXG 2-{[4-(DIETHYLAMINO)PIPERIDIN-1-YL]METHYL}-4-(3-HYDROXYPROP-1-YN-1-YL)-6-IODOPHENOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.60 Å R-free 0.194
4AGO Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan5174 Deposited 2012-01-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES P74 TERT-BUTYL [3-(3-{[4-(DIETHYLAMINO)PIPERIDIN-1-YL]METHYL}-4-HYDROXY-5-IODOPHENYL)PROP-2-YN-1-YL]CARBAMATE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.45 Å R-free 0.217
4AGO Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan5174 Deposited 2012-01-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES P74 TERT-BUTYL [3-(3-{[4-(DIETHYLAMINO)PIPERIDIN-1-YL]METHYL}-4-HYDROXY-5-IODOPHENYL)PROP-2-YN-1-YL]CARBAMATE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.45 Å R-free 0.217
4AGP Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan5176 Deposited 2012-01-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES P51 2-{[4-(diethylamino)piperidin-1-yl]methyl}-6-iodo-4-(3-phenoxyprop-1-yn-1-yl)phenol × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.50 Å R-free 0.187
4AGP Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan5176 Deposited 2012-01-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES P51 2-{[4-(diethylamino)piperidin-1-yl]methyl}-6-iodo-4-(3-phenoxyprop-1-yn-1-yl)phenol × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.50 Å R-free 0.187
4AGQ Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan5196 Deposited 2012-01-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES P96 2-{[4-(diethylamino)piperidin-1-yl]methyl}-6-iodo-4-[3-(phenylamino)prop-1-yn-1-yl]phenol × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 13 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.42 Å R-free 0.192
4AGQ Structure of the p53 core domain mutant Y220C bound to the stabilizing small molecule PhiKan5196 Deposited 2012-01-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES P96 2-{[4-(diethylamino)piperidin-1-yl]methyl}-6-iodo-4-[3-(phenylamino)prop-1-yn-1-yl]phenol × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 13 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.42 Å R-free 0.192
4BUZ SIR2 COMPLEX STRUCTURE MIXTURE OF EX-527 INHIBITOR AND REACTION PRODUCTS OR OF REACTION SUBSTRATES P53 PEPTIDE AND NAD Deposited 2013-06-24 Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain P 379–386（8 aa） Fragment：RESIDUES 379-386
Non-standard monomer：Yes (specific site not provided by mmCIF) OCZ (1S)-6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1- carboxamide × 1 NAD NICOTINAMIDE-ADENINE-DINUCLEOTIDE × 1 OAD 2'-O-ACETYL ADENOSINE-5-DIPHOSPHORIBOSE × 1 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 8.5；8.5
Resolution 1.90 Å R-free 0.194
4BV2 CRYSTAL STRUCTURE OF SIR2 IN COMPLEX WITH THE INHIBITOR EX-527, 2'-O-ACETYL-ADP-RIBOSE AND DEACETYLATED P53-PEPTIDE Deposited 2013-06-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain H 376–388（13 aa） Fragment：RESIDUES 380-384
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.9；20% PEG 6000, 0.1 M BIS-TRIS PH5.9
Resolution 3.30 Å R-free 0.318
4BV2 CRYSTAL STRUCTURE OF SIR2 IN COMPLEX WITH THE INHIBITOR EX-527, 2'-O-ACETYL-ADP-RIBOSE AND DEACETYLATED P53-PEPTIDE Deposited 2013-06-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain E 376–388（13 aa） Fragment：RESIDUES 380-384
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.9；20% PEG 6000, 0.1 M BIS-TRIS PH5.9
Resolution 3.30 Å R-free 0.318
4BV2 CRYSTAL STRUCTURE OF SIR2 IN COMPLEX WITH THE INHIBITOR EX-527, 2'-O-ACETYL-ADP-RIBOSE AND DEACETYLATED P53-PEPTIDE Deposited 2013-06-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain H 376–388（13 aa） Fragment：RESIDUES 380-384
Not recorded ZN ZINC ION × 1 OCZ (1S)-6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1- carboxamide × 1 OAD 2'-O-ACETYL ADENOSINE-5-DIPHOSPHORIBOSE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.9；20% PEG 6000, 0.1 M BIS-TRIS PH5.9
Resolution 3.30 Å R-free 0.318
4BV2 CRYSTAL STRUCTURE OF SIR2 IN COMPLEX WITH THE INHIBITOR EX-527, 2'-O-ACETYL-ADP-RIBOSE AND DEACETYLATED P53-PEPTIDE Deposited 2013-06-24 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain E 376–388（13 aa） Fragment：RESIDUES 380-384
Not recorded ZN ZINC ION × 1 OCZ (1S)-6-chloro-2,3,4,9-tetrahydro-1H-carbazole-1- carboxamide × 1 OAD 2'-O-ACETYL ADENOSINE-5-DIPHOSPHORIBOSE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.9；20% PEG 6000, 0.1 M BIS-TRIS PH5.9
Resolution 3.30 Å R-free 0.318
4FZ3 Crystal structure of SIRT3 in complex with acetyl p53 peptide coupled with 4-amino-7-methylcoumarin Deposited 2012-07-06 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 379–382（4 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；288 K；0.85M HEPES-NA, 8.5%(V/V) ISO-PROPANOL, 17%(W/V) PEG4000, 15%(V/V) GLYCEROL, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 288K
Resolution 2.10 Å R-free 0.282
4HFZ Crystal Structure of an MDM2/P53 Peptide Complex Deposited 2012-10-05 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 15–29（15 aa） Fragment：residues 15-29
Not recorded SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；277 K；0.2 M (NH4)2SO4, pH 4.6 and 30% w/v PEG 8000, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.69 Å R-free 0.247
4HFZ Crystal Structure of an MDM2/P53 Peptide Complex Deposited 2012-10-05 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 15–29（15 aa） Fragment：residues 15-29
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.4；277 K；0.2 M (NH4)2SO4, pH 4.6 and 30% w/v PEG 8000, VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 2.69 Å R-free 0.247
4HJE Crystal structure of p53 core domain in complex with DNA Deposited 2012-10-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 92–291（200 aa） Fragment：UNP residues 92-291
Chain B 92–291（200 aa） Fragment：UNP residues 92-291
Chain C 92–291（200 aa） Fragment：UNP residues 92-291
Chain D 92–291（200 aa） Fragment：UNP residues 92-291
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 1.91 Å R-free 0.228
4IBQ Human p53 core domain with hot spot mutation R273C Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273C ZN ZINC ION × 1 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；20% PEG 3350, 0.1M K-Acetate, 0.1M KF, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.80 Å R-free 0.163
4IBQ Human p53 core domain with hot spot mutation R273C Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273C ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；20% PEG 3350, 0.1M K-Acetate, 0.1M KF, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.80 Å R-free 0.163
4IBQ Human p53 core domain with hot spot mutation R273C Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273C ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；20% PEG 3350, 0.1M K-Acetate, 0.1M KF, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.80 Å R-free 0.163
4IBQ Human p53 core domain with hot spot mutation R273C Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273C ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；20% PEG 3350, 0.1M K-Acetate, 0.1M KF, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.80 Å R-free 0.163
4IBS Human p53 core domain with hot spot mutation R273H (form I) Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273H ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；12% PEG 3350, 0.12M Mg-Formate, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.78 Å R-free 0.181
4IBS Human p53 core domain with hot spot mutation R273H (form I) Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273H ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；12% PEG 3350, 0.12M Mg-Formate, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.78 Å R-free 0.181
4IBS Human p53 core domain with hot spot mutation R273H (form I) Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273H ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；12% PEG 3350, 0.12M Mg-Formate, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.78 Å R-free 0.181
4IBS Human p53 core domain with hot spot mutation R273H (form I) Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273H ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；12% PEG 3350, 0.12M Mg-Formate, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.78 Å R-free 0.181
4IBT Human p53 core domain with hot spot mutation R273H and second-site suppressor mutation T284R Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273H, T284R ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；20% PEG 3350, 0.2M NaF, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.70 Å R-free 0.182
4IBT Human p53 core domain with hot spot mutation R273H and second-site suppressor mutation T284R Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273H, T284R ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；20% PEG 3350, 0.2M NaF, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.70 Å R-free 0.182
4IBT Human p53 core domain with hot spot mutation R273H and second-site suppressor mutation T284R Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273H, T284R ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；20% PEG 3350, 0.2M NaF, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.70 Å R-free 0.182
4IBT Human p53 core domain with hot spot mutation R273H and second-site suppressor mutation T284R Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273H, T284R ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；20% PEG 3350, 0.2M NaF, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.70 Å R-free 0.182
4IBU Human p53 core domain with hot spot mutation R273C and second-site suppressor mutation T284R in sequence-specific complex with DNA Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 94–293（200 aa） Fragment：DNA binding domain
Chain B 94–293（200 aa） Fragment：DNA binding domain
Chain C 94–293（200 aa） Fragment：DNA binding domain
Chain D 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273C, T284R Mutation：R273C, T284R Mutation：R273C, T284R Mutation：R273C, T284R ZN ZINC ION × 4 EDO 1,2-ETHANEDIOL × 16 ACT ACETATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；1:2 PROTEIN/DNA RATIO, 14% PEG 3350, 0.14M Li-Acetate, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 1.70 Å R-free 0.197
4IBV Human p53 core domain with hot spot mutation R273C and second-site suppressor mutation S240R in sequence-specific complex with DNA Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273C, S240R EDO 1,2-ETHANEDIOL × 14 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；1:2.4 PROTEIN/DNA RATIO, 16% PEG 3350, 0.18M NH4F, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 293K
Resolution 2.10 Å R-free 0.229
4IBW Human p53 core domain with hot spot mutation R273H and second-site suppressor mutation T284R in sequence-specific complex with DNA Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273H, T284R ZN ZINC ION × 2 EDO 1,2-ETHANEDIOL × 34 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；1:2.4 PROTEIN/DNA RATIO, 14% PEG 3350, 0.14M NH4F, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.79 Å R-free 0.188
4IBY Human p53 core domain with hot spot mutation R273H and second-site suppressor mutation S240R Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273H, S240R ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；20% PEG 3350, 0.2M Na2HPO4, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.45 Å R-free 0.200
4IBY Human p53 core domain with hot spot mutation R273H and second-site suppressor mutation S240R Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273H, S240R ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；20% PEG 3350, 0.2M Na2HPO4, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.45 Å R-free 0.200
4IBZ Human p53 core domain with hot spot mutation R273C and second-site suppressor mutation T284R Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273C, T284R ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；12% PEG 3350, 0.12M NH4-Acetate, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.92 Å R-free 0.233
4IBZ Human p53 core domain with hot spot mutation R273C and second-site suppressor mutation T284R Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273C, T284R ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 5 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；12% PEG 3350, 0.12M NH4-Acetate, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.92 Å R-free 0.233
4IBZ Human p53 core domain with hot spot mutation R273C and second-site suppressor mutation T284R Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273C, T284R ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；12% PEG 3350, 0.12M NH4-Acetate, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.92 Å R-free 0.233
4IBZ Human p53 core domain with hot spot mutation R273C and second-site suppressor mutation T284R Deposited 2012-12-09 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273C, T284R ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 6 ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；12% PEG 3350, 0.12M NH4-Acetate, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.92 Å R-free 0.233
4IJT Human p53 core domain with hot spot mutation R273H (form II) Deposited 2012-12-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa） Fragment：DNA binding domain
Mutation：R273H ZN ZINC ION × 2 DTT 2,3-DIHYDROXY-1,4-DITHIOBUTANE × 1 EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.1；293 K；1:1.5 PROTEIN/DNA RATIO, 20% PEG 3350, 0.2M KCl, pH 6.1, Vapor diffusion, hanging drop, temperature 293K
Resolution 1.78 Å R-free 0.194
4KVP Human p53 Core Domain Mutant V157F Deposited 2013-05-22 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：p53 Core Domain
Mutation：V157F ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；277 K；2 microliter protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliter reservoir buffer (25% (w/v) polyethylene glycol (PEG) 2000 monomethyl ether (MME)), pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.50 Å R-free 0.210
4KVP Human p53 Core Domain Mutant V157F Deposited 2013-05-22 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：p53 Core Domain
Mutation：V157F ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；277 K；2 microliter protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliter reservoir buffer (25% (w/v) polyethylene glycol (PEG) 2000 monomethyl ether (MME)), pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.50 Å R-free 0.210
4KVP Human p53 Core Domain Mutant V157F Deposited 2013-05-22 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–312（219 aa） Fragment：p53 Core Domain
Mutation：V157F ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；277 K；2 microliter protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliter reservoir buffer (25% (w/v) polyethylene glycol (PEG) 2000 monomethyl ether (MME)), pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.50 Å R-free 0.210
4KVP Human p53 Core Domain Mutant V157F Deposited 2013-05-22 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–312（219 aa） Fragment：p53 Core Domain
Mutation：V157F ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.6；277 K；2 microliter protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliter reservoir buffer (25% (w/v) polyethylene glycol (PEG) 2000 monomethyl ether (MME)), pH 7.6, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 1.50 Å R-free 0.210
4LO9 Human p53 Core Domain Mutant N235K Deposited 2013-07-12 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：p53 Core Domain (UNP residues 94-312)
Mutation：N235K ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；2 microliter protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliter reservoir buffer(100 mM HEPES, 30 % (w/v) polyethylene glycol (PEG) 6000, pH 7.0), VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.50 Å R-free 0.247
4LO9 Human p53 Core Domain Mutant N235K Deposited 2013-07-12 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：p53 Core Domain (UNP residues 94-312)
Mutation：N235K ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；2 microliter protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliter reservoir buffer(100 mM HEPES, 30 % (w/v) polyethylene glycol (PEG) 6000, pH 7.0), VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.50 Å R-free 0.247
4LO9 Human p53 Core Domain Mutant N235K Deposited 2013-07-12 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–312（219 aa） Fragment：p53 Core Domain (UNP residues 94-312)
Mutation：N235K ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；2 microliter protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliter reservoir buffer(100 mM HEPES, 30 % (w/v) polyethylene glycol (PEG) 6000, pH 7.0), VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.50 Å R-free 0.247
4LO9 Human p53 Core Domain Mutant N235K Deposited 2013-07-12 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–312（219 aa） Fragment：p53 Core Domain (UNP residues 94-312)
Mutation：N235K ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；277 K；2 microliter protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliter reservoir buffer(100 mM HEPES, 30 % (w/v) polyethylene glycol (PEG) 6000, pH 7.0), VAPOR DIFFUSION, HANGING DROP, temperature 277K
Resolution 2.50 Å R-free 0.247
4LOE Human p53 Core Domain Mutant N239Y Deposited 2013-07-12 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：p53 Core Domain (UNP residues 94-312)
Mutation：N239Y ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；277 K；2 microliter protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliter reservoir buffer(200 mM lithium acetate, 20% (w/v) PEG 3350), VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.85 Å R-free 0.244
4LOE Human p53 Core Domain Mutant N239Y Deposited 2013-07-12 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：p53 Core Domain (UNP residues 94-312)
Mutation：N239Y ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；277 K；2 microliter protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliter reservoir buffer(200 mM lithium acetate, 20% (w/v) PEG 3350), VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.85 Å R-free 0.244
4LOE Human p53 Core Domain Mutant N239Y Deposited 2013-07-12 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–312（219 aa） Fragment：p53 Core Domain (UNP residues 94-312)
Mutation：N239Y ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；277 K；2 microliter protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliter reservoir buffer(200 mM lithium acetate, 20% (w/v) PEG 3350), VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.85 Å R-free 0.244
4LOE Human p53 Core Domain Mutant N239Y Deposited 2013-07-12 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–312（219 aa） Fragment：p53 Core Domain (UNP residues 94-312)
Mutation：N239Y ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.6；277 K；2 microliter protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliter reservoir buffer(200 mM lithium acetate, 20% (w/v) PEG 3350), VAPOR DIFFUSION, SITTING DROP, temperature 277K
Resolution 1.85 Å R-free 0.244
4LOF Human p53 Core Domain Mutant V157F/N235K/N239Y Deposited 2013-07-12 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：p53 Core Domain (UNP residues 94-312)
Mutation：V157F, N235K, N239Y ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7.6；2 microliters protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliters reservoir buffer with 200 mM di-sodium hydrogen phosphate dehydrate (Na2HPO4), 20% (w/v) PEG 3350, VAPOR DIFFUSION
Resolution 2.00 Å R-free 0.256
4MZI Crystal structure of a human mutant p53 Deposited 2013-09-30 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–292（199 aa） Fragment：UNP residues 94-292
Mutation：S121F, V122G ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.8；278 K；pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 278K
Resolution 1.25 Å R-free 0.201
4MZR Crystal structure of a polypeptide p53 mutant bound to DNA Deposited 2013-09-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 94–358（265 aa） Fragment：UNP residues 94-358
Chain B 94–358（265 aa） Fragment：UNP residues 94-358
Chain C 94–358（265 aa） Fragment：UNP residues 94-358
Chain D 94–358（265 aa） Fragment：UNP residues 94-358
Mutation：S121F, V122G Mutation：S121F, V122G Mutation：S121F, V122G Mutation：S121F, V122G ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；278 K；0.2M potassium sodium tartrate tetrahydrate, 20% PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 278K
Resolution 2.90 Å R-free 0.281
4QO1 p53 DNA binding domain in complex with Nb139 Deposited 2014-06-19 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 92–312（221 aa） Fragment：p53DBD, unp residues 92-312
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；293 K；Crystals of the complex were obtained at 293K using the hanging-drop vapour diffusion method after mixing 1:l protein solution with 1:l reservoir solution equilibrated against 125 ul 0.2 M potassium formate 20% w/v PEG 3350 reservoir solution, pH 6.5, VAPOR DIFFUSION, HANGING DROP
Resolution 1.92 Å R-free 0.205
4RP6 Structure of the amyloid-forming segment LTIITLE from p53 (residues 252-258) Deposited 2014-10-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain Z 252–258（7 aa） Fragment：UNP residues 252-258
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；291 K；reservoir contained 0.1 M Tris buffer pH 8.5 and 20% ethanol, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 1.70 Å R-free 0.192
4RP7 Structure of the amyloid-forming segment TIITLE from p53 (residues 253-258) Deposited 2014-10-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric
Chain Z 253–258（6 aa） Fragment：UNP residues 253-258
Not recorded ZN ZINC ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；291 K；reservoir contained 0.01 M zinc chloride, 0.1 M MES buffer pH 6, and 20% PEG 6000, VAPOR DIFFUSION, HANGING DROP, temperature 291K
Resolution 1.58 Å R-free 0.193
4XR8 Crystal structure of the HPV16 E6/E6AP/p53 ternary complex at 2.25 A resolution Deposited 2015-01-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 55–253（199 aa）
Not recorded PEG DI(HYDROXYETHYL)ETHER × 2 ZN ZINC ION × 3 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；290 K；7.5 % PEG 20K, 0.05 M MES pH 6.5
Resolution 2.25 Å R-free 0.246
4XR8 Crystal structure of the HPV16 E6/E6AP/p53 ternary complex at 2.25 A resolution Deposited 2015-01-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain D 55–253（199 aa）
Not recorded PEG DI(HYDROXYETHYL)ETHER × 2 ZN ZINC ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；290 K；7.5 % PEG 20K, 0.05 M MES pH 6.5
Resolution 2.25 Å R-free 0.246
5A7B Structure of the p53 cancer Y220C bound to the stabilizing small molecule PhiKan5211 Deposited 2015-07-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 KMN 2-[[4-(diethylamino)piperidin-1-yl]methyl]-6-ethynyl-4-(3-phenoxyprop-1-ynyl)phenol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；CRYSTALLIZATION CONDITIONS: SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.40 Å R-free 0.192
5A7B Structure of the p53 cancer Y220C bound to the stabilizing small molecule PhiKan5211 Deposited 2015-07-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 KMN 2-[[4-(diethylamino)piperidin-1-yl]methyl]-6-ethynyl-4-(3-phenoxyprop-1-ynyl)phenol × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；CRYSTALLIZATION CONDITIONS: SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.40 Å R-free 0.192
5AB9 Structure of the p53 cancer mutant Y220C with bound small molecule 7- ethyl-3-(piperidin-4-yl)-1H-indole Deposited 2015-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 92O 7-ethyl-3-(piperidin-4-yl)-1H-indole × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 40 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.36 Å R-free 0.166
5AB9 Structure of the p53 cancer mutant Y220C with bound small molecule 7- ethyl-3-(piperidin-4-yl)-1H-indole Deposited 2015-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 92O 7-ethyl-3-(piperidin-4-yl)-1H-indole × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 40 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.36 Å R-free 0.166
5ABA Structure of the p53 cancer mutant Y220C with bound small-molecule stabilizer PhiKan5149 Deposited 2015-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 UL7 1-{1-[(3-bromo-5-chloro-2-hydroxyphenyl)methyl piperidin-4-yl}piperidin-4-ol] × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.62 Å R-free 0.203
5ABA Structure of the p53 cancer mutant Y220C with bound small-molecule stabilizer PhiKan5149 Deposited 2015-08-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 UL7 1-{1-[(3-bromo-5-chloro-2-hydroxyphenyl)methyl piperidin-4-yl}piperidin-4-ol] × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.62 Å R-free 0.203
5AOI Structure of the p53 cancer mutant Y220C in complex with an indole- based small molecule Deposited 2015-09-10 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.78 Å R-free 0.206
5AOI Structure of the p53 cancer mutant Y220C in complex with an indole- based small molecule Deposited 2015-09-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 RZH 2-(5-BROMO-7-ETHYL-2-METHYL-1H-INDOLE-3-YL)ETHAN-1-AMIN × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.78 Å R-free 0.206
5AOJ Structure of the p53 cancer mutant Y220C in complex with 2-hydroxy-3, 5-diiodo-4-(1H-pyrrol-1-yl)benzoic acid Deposited 2015-09-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES Y0V 2-hydroxy-3,5-diiodo-4-(1H-pyrrol-1-yl)benzoic acid × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 23 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.47 Å R-free 0.178
5AOJ Structure of the p53 cancer mutant Y220C in complex with 2-hydroxy-3, 5-diiodo-4-(1H-pyrrol-1-yl)benzoic acid Deposited 2015-09-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES Y0V 2-hydroxy-3,5-diiodo-4-(1H-pyrrol-1-yl)benzoic acid × 1 ZN ZINC ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 23 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.47 Å R-free 0.178
5AOK Structure of the p53 cancer mutant Y220C with bound small molecule PhiKan7099 Deposited 2015-09-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 GOL GLYCEROL × 1 GOH 5-[2-cyclopropyl-5-(1H-pyrrol-1-yl)-1,3-oxazol-4-yl]-1H-1,2,3,4-tetrazole × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 38 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.35 Å R-free 0.169
5AOK Structure of the p53 cancer mutant Y220C with bound small molecule PhiKan7099 Deposited 2015-09-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 GOL GLYCEROL × 1 GOH 5-[2-cyclopropyl-5-(1H-pyrrol-1-yl)-1,3-oxazol-4-yl]-1H-1,2,3,4-tetrazole × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 38 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.35 Å R-free 0.169
5AOL Structure of the p53 cancer mutant Y220C with bound 3-bromo-5-(trifluoromethyl)benzene-1,2-diamine Deposited 2015-09-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES UFV 3-BROMO-5-(TRIFLUOROMETHYL)BENZENE-1,2-DIAMINE × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.50 Å R-free 0.169
5AOL Structure of the p53 cancer mutant Y220C with bound 3-bromo-5-(trifluoromethyl)benzene-1,2-diamine Deposited 2015-09-10 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 MM COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.50 Å R-free 0.169
5AOM Structure of the p53 cancer mutant Y220C with bound small molecule PhiKan883 Deposited 2015-09-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES FY8 N-(5-chloranyl-2-oxidanyl-phenyl)piperidine-4-carboxamide × 2 GOL GLYCEROL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.74 Å R-free 0.191
5AOM Structure of the p53 cancer mutant Y220C with bound small molecule PhiKan883 Deposited 2015-09-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES FY8 N-(5-chloranyl-2-oxidanyl-phenyl)piperidine-4-carboxamide × 2 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.74 Å R-free 0.191
5BUA Lysine 120-acetylated P53 DNA binding domain in a complex with DNA. Deposited 2015-06-03 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 94–293（200 aa） Fragment：P53 DNA binding domain, UNP residues 94-293
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.1；286 K；0.2M Ammonium fluoride; 20% PEG 3350
Resolution 1.81 Å R-free 0.213
5ECG Crystal structure of the BRCT domains of 53BP1 in complex with p53 and H2AX-pSer139 (gammaH2AX) Deposited 2015-10-20 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain A 95–312（218 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；200mM NaF, 100mM Bis-Tris Propane pH 6.5, 20% (w/v) PEG 3,350
Resolution 3.00 Å R-free 0.264
5ECG Crystal structure of the BRCT domains of 53BP1 in complex with p53 and H2AX-pSer139 (gammaH2AX) Deposited 2015-10-20 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 95–312（218 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293 K；200mM NaF, 100mM Bis-Tris Propane pH 6.5, 20% (w/v) PEG 3,350
Resolution 3.00 Å R-free 0.264
5G4M Crystal structure of the p53 cancer mutant Y220C in complex with a monofluorinated derivative of the small molecule stabilizer Phikan083 Deposited 2016-05-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 O82 1-[9-(2-fluoroethyl)-9H-carbazol-3-yl]-N-methylmethanamine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.38 Å R-free 0.170
5G4M Crystal structure of the p53 cancer mutant Y220C in complex with a monofluorinated derivative of the small molecule stabilizer Phikan083 Deposited 2016-05-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, UNP RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 O82 1-[9-(2-fluoroethyl)-9H-carbazol-3-yl]-N-methylmethanamine × 1 GOL GLYCEROL × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.38 Å R-free 0.170
5G4N Crystal structure of the p53 cancer mutant Y220C in complex with a difluorinated derivative of the small molecule stabilizer Phikan083 Deposited 2016-05-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 O83 1-[9-(2,2-difluoroethyl)-9H-carbazol-3-yl]-N-methylmethanamine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL
Resolution 1.35 Å R-free 0.168
5G4N Crystal structure of the p53 cancer mutant Y220C in complex with a difluorinated derivative of the small molecule stabilizer Phikan083 Deposited 2016-05-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 O83 1-[9-(2,2-difluoroethyl)-9H-carbazol-3-yl]-N-methylmethanamine × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL
Resolution 1.35 Å R-free 0.168
5G4O Crystal structure of the p53 cancer mutant Y220C in complex with a trifluorinated derivative of the small molecule stabilizer Phikan083 Deposited 2016-05-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 O80 N,N-dimethyl-1-[9-(2,2,2-trifluoroethyl)-9H-carbazol-3-yl]methanamine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.48 Å R-free 0.171
5G4O Crystal structure of the p53 cancer mutant Y220C in complex with a trifluorinated derivative of the small molecule stabilizer Phikan083 Deposited 2016-05-13 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 94-312
Mutation：YES ZN ZINC ION × 1 O80 N,N-dimethyl-1-[9-(2,2,2-trifluoroethyl)-9H-carbazol-3-yl]methanamine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；SITTING-DROP VAPOR DIFFUSION AT 21 DEGREE C. PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: SATURATED SOLUTION OF COMPOUND IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.48 Å R-free 0.171
5HOU Solution Structure of p53TAD-TAZ1 Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–61（61 aa） Fragment：p53TAD, TAZ1 domain of CBP
Not recorded ZN ZINC ION × 3 SOLUTION NMR
NMR measurement conditions pH 6.8；308 K；Ionic strength (raw mmCIF value) 50；Pressure 1
NMR measurement conditions pH 6.4；308 K；Ionic strength (raw mmCIF value) 50；Pressure 1
NMR sample composition 1.0 mM [U-15N] p53TAD - [NA] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 95% H2O, 5% D2O | 95% H2O/5% D2O
NMR sample composition 1.0 mM [U-15N][U-13C] p53TAD - [NA] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O | 99% D2O, 1% H2O
NMR sample composition 1.0 mM [NA] p53TAD - [U-15N] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 1.0 mM [NA] p53TAD - [U-15N][U-13C] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O | 99% D2O, 1% H2O
NMR sample composition 1.0 mM [U-15N][U-13C] p53TAD - [NA] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 95% H2O/5% D2O | 95% H2O/5% D2O
NMR sample composition 1 mM [NA] p53TAD - [U-15N][U-13C] TAZ1 p53TAD-TAZ1 fusion protein, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 95% H2O/5% D2O | 95% H2O/5% D2O
Resolution not provided
5HP0 Solution Structure of TAZ2-p53AD2 Deposited 2016-01-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 37–61（25 aa） Fragment：p53AD2, TAZ2 domain of CBP
Not recorded ZN ZINC ION × 3 SOLUTION NMR
NMR measurement conditions pH 6.8；305 K；Ionic strength (raw mmCIF value) 50；Pressure 1
NMR measurement conditions pH 6.4；305 K；Ionic strength (raw mmCIF value) 50；Pressure 1
NMR sample composition 1 mM [U-13C; U-15N] TAZ2-p53AD2, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 10 % [U-2H] D2O, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM [U-13C; U-15N] TAZ2-p53AD2, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O | 99% D2O, 1% H2O
NMR sample composition 1 mM [U-13C; U-15N] TAZ2-p53AD2, 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 5 % [U-2H] D2O, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM [U-13C] TAZ2, 1 mM p53AD2(38-61), 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 5 % [U-2H] D2O, 99% D2O, 1% H2O | 99% D2O, 1% H2O
NMR sample composition 1 mM [U-13C] p53AD2, 1 mM TAZ2, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O | 99% D2O, 1% H2O
Resolution not provided
5HPD Solution Structure of TAZ2-p53TAD Deposited 2016-01-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 2–61（60 aa） Fragment：p53TAD, TAZ2 domain of CBP
Not recorded ZN ZINC ION × 3 SOLUTION NMR
NMR measurement conditions pH 6.8；305 K；Ionic strength (raw mmCIF value) 50；Pressure 1
NMR measurement conditions pH 6.4；305 K；Ionic strength (raw mmCIF value) 50；Pressure 1
NMR sample composition 1.75 mM [U-13C; U-15N] TAZ2-p53TAD, 20 mM TRIS, 50 mM sodium chloride, 1 mM DTT, 10 % [U-2H] D2O, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1.75 mM [U-13C; U-15N] TAZ2-p53TAD, 20 mM [U-2H] TRIS, 50 mM sodium chloride, 1 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O | 99% D2O, 1% H2O
NMR sample composition 1 mM [U-13C] TAZ2, 1 mM p53(13-37, 1 mM p53(38-61), 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 20 mM [U-2H] TRIS, 99% D2O, 1% H2O | 99% D2O, 1% H2O
NMR sample composition 1 mM TAZ2, 1 mM [U-13C] p53(13-37), 1 mM [U-13C] p53(38-61), 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O | 99% D2O, 1% H2O
NMR sample composition 1 mM TAZ2, 1 mM [U-15N] p53(13-61), 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 10 % [U-2H] D2O, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM [U-15N] TAZ2, 1 mM p53(13-61), 20 mM TRIS, 50 mM sodium chloride, 2 mM DTT, 10 % [U-2H] D2O, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 1 mM TAZ2, 1 mM [U-13C] p53(13-61), 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O | 99% D2O, 1% H2O
NMR sample composition 1 mM [U-13C] TAZ2, 1 mM p53(13-61), 20 mM [U-2H] TRIS, 50 mM sodium chloride, 2 mM [U-2H] DTT, 99 % [U-2H] D2O, 99% D2O, 1% H2O | 99% D2O, 1% H2O
Resolution not provided
5LAP p53 cancer mutant Y220C with Cys182 alkylation Deposited 2016-06-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 6SM 5-chloranylpyrimidine-4-carboxylic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 mM Phikan11000 IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.42 Å R-free 0.193
5LAP p53 cancer mutant Y220C with Cys182 alkylation Deposited 2016-06-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 6SM 5-chloranylpyrimidine-4-carboxylic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；PROTEIN SOLUTION: 6 MG/ML PROTEIN IN 25 MM SODIUM PHOSPHATE, PH 7.2, 150 MM KCL, 5 MM DTT. RESERVOIR BUFFER: 100 MM HEPES, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 5 MM DTT. SOAKING BUFFER: 30 mM Phikan11000 IN 100 MM HEPES, PH 7.2, 10 MM SODIUM PHOSPHATE, PH 7.2, 19% (W/V) POLYETHYLENE GLYCOL 4000, 20 % (V/V) GLYCEROL, 150 MM KCL.
Resolution 1.42 Å R-free 0.193
5LGY Lysine 120-acetylated P53 DNA binding domain in a complex with the BAX response element. Deposited 2016-07-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 94–291（198 aa） Fragment：UNP residues 94-291
Chain B 94–291（198 aa） Fragment：UNP residues 94-291
Chain C 94–291（198 aa） Fragment：UNP residues 94-291
Chain D 94–291（198 aa） Fragment：UNP residues 94-291
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.1；286 K；0.22 M Ammonium acetate, 10% w/v PEG 3350, tri-Sodium citrate pH 6.1
Resolution 2.92 Å R-free 0.277
5MCT New Insights into the Role of DNA Shape on Its Recognition by p53 Proteins (complex p53DBD-LHG1) Deposited 2016-11-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 94–293（200 aa） Fragment：P53 DNA BINDING DOMAIN
Chain B 94–293（200 aa） Fragment：P53 DNA BINDING DOMAIN
Not recorded ZN ZINC ION × 4 EDO 1,2-ETHANEDIOL × 12 FOR FORMYL GROUP × 4 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7；292 K；0.1 M Ammonium citrate, 12% w/v Polyethylene glycol 3,350
Resolution 1.45 Å R-free 0.189
5MCU New Insights into the Role of DNA Shape on Its Recognition by p53 Proteins (complex p53DBD-LHG2) Deposited 2016-11-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 94–293（200 aa） Fragment：P53 DNA BINDING DOMAIN
Chain B 94–293（200 aa） Fragment：P53 DNA BINDING DOMAIN
Not recorded ZN ZINC ION × 4 EDO 1,2-ETHANEDIOL × 12 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7；292 K；0.05 M HEPES sodium salt, 12% w/v Polyethylene glycol 3,350
Resolution 1.70 Å R-free 0.201
5MCV New Insights into the Role of DNA Shape on Its Recognition by p53 Proteins (complex p53DBD-LWC1) Deposited 2016-11-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 55–254（200 aa） Fragment：P53 DNA BINDING DOMAIN
Chain B 55–254（200 aa） Fragment：P53 DNA BINDING DOMAIN
Not recorded ZN ZINC ION × 4 EDO 1,2-ETHANEDIOL × 20 ACT ACETATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 8.8；292 K；0.02 M Citric acid, 0.08 M BIS-TRIS propane, 16% w/v Polyethylene glycol 3,350
Resolution 1.60 Å R-free 0.188
5MCW New Insights into the Role of DNA Shape on Its Recognition by p53 Proteins (complex p53DBD-LWC2) Deposited 2016-11-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 94–293（200 aa） Fragment：P53 DNA BINDING DOMAIN
Chain B 94–293（200 aa） Fragment：P53 DNA BINDING DOMAIN
Not recorded ZN ZINC ION × 4 FOR FORMYL GROUP × 4 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 8.8；292 K；0.02 M Citric acid, 0.08 M BIS-TRIS propane, 18% w/v Polyethylene glycol 3,350
Resolution 1.90 Å R-free 0.235
5MF7 New Insights into the Role of DNA Shape on Its Recognition by p53 Proteins (complex p53DBD-GADD45) Deposited 2016-11-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 55–254（200 aa） Fragment：P53 DNA BINDING DOMAIN
Chain B 55–254（200 aa） Fragment：P53 DNA BINDING DOMAIN
Not recorded ZN ZINC ION × 4 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 8；292 K；4% Tacsimate, 12% w/v Polyethylene glycol 3,350
Resolution 1.59 Å R-free 0.233
5MG7 New Insights into the Role of DNA Shape on Its Recognition by p53 Proteins (complex p53DBD-p53R2) Deposited 2016-11-21 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 94–293（200 aa） Fragment：P53 DNA Binding Domain, UNP Residues 94-293
Chain B 94–293（200 aa） Fragment：P53 DNA Binding Domain, UNP Residues 94-293
Not recorded ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7；292 K；0.07 M ammonium tartrate dibasic, 8.4% Polyethylene glycol 3,350
Resolution 1.45 Å R-free 0.202
5O1A p53 cancer mutant Y220C in complex with compound MB240 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9H5 [3,5-bis(iodanyl)-2-oxidanyl-4-pyrrol-1-yl-phenyl]-(4-methylpiperazin-1-yl)methanone × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.44 Å R-free 0.178
5O1A p53 cancer mutant Y220C in complex with compound MB240 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9H5 [3,5-bis(iodanyl)-2-oxidanyl-4-pyrrol-1-yl-phenyl]-(4-methylpiperazin-1-yl)methanone × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.44 Å R-free 0.178
5O1B p53 cancer mutant Y220C in complex with compound MB84 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9H2 6-(hydroxymethyl)-2,4-bis(iodanyl)-3-pyrrol-1-yl-phenol × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.43 Å R-free 0.174
5O1B p53 cancer mutant Y220C in complex with compound MB84 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9H2 6-(hydroxymethyl)-2,4-bis(iodanyl)-3-pyrrol-1-yl-phenol × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.43 Å R-free 0.174
5O1C p53 cancer mutant Y220C in complex with compound MB184 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9GZ 5-(4-fluorophenyl)-3-iodanyl-2-oxidanyl-4-pyrrol-1-yl-benzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.32 Å R-free 0.172
5O1C p53 cancer mutant Y220C in complex with compound MB184 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9GZ 5-(4-fluorophenyl)-3-iodanyl-2-oxidanyl-4-pyrrol-1-yl-benzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.32 Å R-free 0.172
5O1D p53 cancer mutant Y220C in complex with compound MB481 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9GW 3-iodanyl-2-oxidanyl-5-propoxy-4-pyrrol-1-yl-benzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.36 Å R-free 0.164
5O1D p53 cancer mutant Y220C in complex with compound MB481 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9GW 3-iodanyl-2-oxidanyl-5-propoxy-4-pyrrol-1-yl-benzoic acid × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.36 Å R-free 0.164
5O1E p53 cancer mutant Y220C im complex with compound MB577 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9GT 3-iodanyl-2-oxidanyl-5-prop-2-enoxy-4-pyrrol-1-yl-benzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.30 Å R-free 0.165
5O1E p53 cancer mutant Y220C im complex with compound MB577 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9GT 3-iodanyl-2-oxidanyl-5-prop-2-enoxy-4-pyrrol-1-yl-benzoic acid × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.30 Å R-free 0.165
5O1F p53 cancer mutant Y220C in complex with compound MB582 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9GQ 5-butoxy-3-iodanyl-2-oxidanyl-4-pyrrol-1-yl-benzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.38 Å R-free 0.167
5O1F p53 cancer mutant Y220C in complex with compound MB582 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9GQ 5-butoxy-3-iodanyl-2-oxidanyl-4-pyrrol-1-yl-benzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.38 Å R-free 0.167
5O1G p53 cancer mutant Y220C in complex with compound MB487 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9GK 3-iodanyl-2-oxidanyl-5-(2-phenylethoxy)-4-pyrrol-1-yl-benzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.35 Å R-free 0.166
5O1G p53 cancer mutant Y220C in complex with compound MB487 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9GK 3-iodanyl-2-oxidanyl-5-(2-phenylethoxy)-4-pyrrol-1-yl-benzoic acid × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.35 Å R-free 0.166
5O1H p53 cancer mutant Y220C in complex with compound MB539 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9GN 3-iodanyl-2-oxidanyl-5-propylsulfanyl-4-pyrrol-1-yl-benzoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.32 Å R-free 0.160
5O1H p53 cancer mutant Y220C in complex with compound MB539 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9GN 3-iodanyl-2-oxidanyl-5-propylsulfanyl-4-pyrrol-1-yl-benzoic acid × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 30 mM compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.32 Å R-free 0.160
5O1I p53 cancer mutant Y220C in complex with compound MB710 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 9GH 2-(diethylamino)-6-iodanyl-5-oxidanyl-7-pyrrol-1-yl-1,3-benzothiazole-4-carboxylic acid × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.40 Å R-free 0.187
5O1I p53 cancer mutant Y220C in complex with compound MB710 Deposited 2017-05-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：UNP residues 94-312
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.40 Å R-free 0.187
5OL0 Structure of Leishmania infantum Silent Information Regulator 2 related protein 1 (LiSIR2rp1) in complex with acetylated p53 peptide Deposited 2017-07-26 Different construct Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 372–389（18 aa） Fragment：UNP residues 372-389
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；100mM Na Hepes pH7.5; 25% PEG2000 MME
Resolution 1.99 Å R-free 0.226
5OL0 Structure of Leishmania infantum Silent Information Regulator 2 related protein 1 (LiSIR2rp1) in complex with acetylated p53 peptide Deposited 2017-07-26 Different construct Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 372–389（18 aa） Fragment：UNP residues 372-389
Non-standard monomer：Yes (specific site not provided by mmCIF) ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；295 K；100mM Na Hepes pH7.5; 25% PEG2000 MME
Resolution 1.99 Å R-free 0.226
5XZC Cryo-EM structure of p300-p53 protein complex Deposited 2017-07-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain B 92–356（265 aa）
Chain C 92–356（265 aa）
Chain D 92–356（265 aa）
Chain E 92–356（265 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 10.70 Å
6FF9 Mutant R280K of human P53 Deposited 2018-01-04 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 58–250（193 aa）
Mutation：R280K ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；35% PEG 3350
Resolution 2.00 Å R-free 0.226
6FF9 Mutant R280K of human P53 Deposited 2018-01-04 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 58–250（193 aa）
Mutation：R280K ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；35% PEG 3350
Resolution 2.00 Å R-free 0.226
6FF9 Mutant R280K of human P53 Deposited 2018-01-04 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 58–250（193 aa）
Mutation：R280K ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；35% PEG 3350
Resolution 2.00 Å R-free 0.226
6FF9 Mutant R280K of human P53 Deposited 2018-01-04 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 58–250（193 aa）
Mutation：R280K ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；35% PEG 3350
Resolution 2.00 Å R-free 0.226
6FJ5 New Insights into the Role of DNA Shape on Its Recognition by p53 Proteins (complex p53DBD-AGG-HG) Deposited 2018-01-20 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 94–293（200 aa） Fragment：P53 DNA BINDING DOMAIN, UNP residues 94-293
Chain B 94–293（200 aa） Fragment：P53 DNA BINDING DOMAIN, UNP residues 94-293
Chain C 94–293（200 aa） Fragment：P53 DNA BINDING DOMAIN, UNP residues 94-293
Chain D 94–293（200 aa） Fragment：P53 DNA BINDING DOMAIN, UNP residues 94-293
Not recorded ZN ZINC ION × 4 EDO 1,2-ETHANEDIOL × 14 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 7；292 K；0.1 M Sodium formate pH 7.0, 12% w/v Polyethylene glycol 3,350
Resolution 2.05 Å R-free 0.244
6GGA p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9284 Deposited 2018-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：M133L, V203A, Y220C, N239Y, N268D EY2 (7-bromanyl-9-ethyl-carbazol-3-yl)methyl-methyl-azanium × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.55 Å R-free 0.200
6GGA p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9284 Deposited 2018-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：M133L, V203A, Y220C, N239Y, N268D EY2 (7-bromanyl-9-ethyl-carbazol-3-yl)methyl-methyl-azanium × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.55 Å R-free 0.200
6GGB p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9318 Deposited 2018-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded ZN ZINC ION × 1 EXQ [9-ethyl-7-(4-methylthiophen-2-yl)carbazol-3-yl]methyl-methyl-azanium × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.32 Å R-free 0.161
6GGB p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9318 Deposited 2018-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded ZN ZINC ION × 1 EXQ [9-ethyl-7-(4-methylthiophen-2-yl)carbazol-3-yl]methyl-methyl-azanium × 1 GOL GLYCEROL × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.32 Å R-free 0.161
6GGC p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9320 Deposited 2018-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 EXN [9-ethyl-7-(furan-2-yl)carbazol-3-yl]methyl-methyl-azanium × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.24 Å R-free 0.166
6GGC p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9320 Deposited 2018-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 EXN [9-ethyl-7-(furan-2-yl)carbazol-3-yl]methyl-methyl-azanium × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.24 Å R-free 0.166
6GGD p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9324 Deposited 2018-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：M133L, V203A, Y220C, N239Y, N268D, ZN ZINC ION × 1 EYB [9-ethyl-7-(1,2-oxazol-4-yl)carbazol-3-yl]methyl-methyl-azanium × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.40 Å R-free 0.170
6GGD p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9324 Deposited 2018-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：M133L, V203A, Y220C, N239Y, N268D, ZN ZINC ION × 1 EYB [9-ethyl-7-(1,2-oxazol-4-yl)carbazol-3-yl]methyl-methyl-azanium × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.40 Å R-free 0.170
6GGE p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9327 Deposited 2018-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：M133L, V203A, Y220S,N239Y, N268D ZN ZINC ION × 1 EYE [9-ethyl-7-(5-methylthiophen-2-yl)carbazol-3-yl]methyl-methyl-azanium × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.25 Å R-free 0.171
6GGE p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9327 Deposited 2018-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：M133L, V203A, Y220S,N239Y, N268D ZN ZINC ION × 1 EYE [9-ethyl-7-(5-methylthiophen-2-yl)carbazol-3-yl]methyl-methyl-azanium × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.25 Å R-free 0.171
6GGF Structure of the p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9328 Deposited 2018-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 EXQ [9-ethyl-7-(4-methylthiophen-2-yl)carbazol-3-yl]methyl-methyl-azanium × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm NaCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm NaCl.
Resolution 1.32 Å R-free 0.171
6GGF Structure of the p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9328 Deposited 2018-05-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 EXQ [9-ethyl-7-(4-methylthiophen-2-yl)carbazol-3-yl]methyl-methyl-azanium × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm NaCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of compound in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm NaCl.
Resolution 1.32 Å R-free 0.171
6LHD Crystal structure of p53/BCL-xL fusion complex Deposited 2019-12-07 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 57–253（197 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；0.2M sodium malonate pH 7.0, 20%(w/v) polyethylene glycol 3,350
Resolution 2.50 Å R-free 0.260
6LHD Crystal structure of p53/BCL-xL fusion complex Deposited 2019-12-07 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain B 57–253（197 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291.15 K；0.2M sodium malonate pH 7.0, 20%(w/v) polyethylene glycol 3,350
Resolution 2.50 Å R-free 0.260
6RJZ Fragment AZ-015 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-04-29 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 4 CL CHLORIDE ION × 2 GOL GLYCEROL × 2 K6B 7-(6-azanylpyridin-2-yl)-1-benzothiophene-2-carboximidamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.58 Å R-free 0.218
6RK8 Fragment AZ-014 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-04-30 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 4 CL CHLORIDE ION × 2 K6N 7-(3-azanyl-4-methyl-pyrazol-1-yl)-1-benzothiophene-2-carboximidamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.60 Å R-free 0.229
6RKI Fragment AZ-023 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-04-30 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 4 CL CHLORIDE ION × 2 K6T 5-[(3-aminophenyl)amino]-4-phenyl-thiophene-2-carboximidamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.88 Å R-free 0.206
6RKK Fragment AZ-021 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-04-30 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 4 CL CHLORIDE ION × 2 GOL GLYCEROL × 2 K6W 4-phenyl-5-(phenylmethyl)thiophene-2-carboximidamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.88 Å R-free 0.272
6RKM Fragment AZ-022 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-04-30 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 2 CL CHLORIDE ION × 2 GOL GLYCEROL × 2 K6Z 4-phenyl-5-phenylazanyl-thiophene-2-carboximidamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.88 Å R-free 0.230
6RL3 Fragment AZ-003 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-05-01 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 4 CL CHLORIDE ION × 2 GOL GLYCEROL × 2 K48 5-azanyl-4-phenyl-thiophene-2-carboximidamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.30 Å R-free 0.192
6RL4 Fragment AZ-025 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-05-01 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 4 CL CHLORIDE ION × 2 K7N 5-[1-(2-azanylethyl)imidazol-4-yl]-4-phenyl-thiophene-2-carboximidamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.60 Å R-free 0.180
6RL6 Fragment AZ-024 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-05-01 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 2 CL CHLORIDE ION × 2 K7Q ~{N}-(2-azanylethyl)-2-carbamimidoyl-7-methoxy-1-benzothiophene-4-carboxamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.60 Å R-free 0.183
6RM5 Fragment AZ-016 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-05-05 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 6 CL CHLORIDE ION × 2 K8W 7-(6-azanyl-5-methyl-pyridin-2-yl)-1-benzothiophene-2-carboximidamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.88 Å R-free 0.207
6RM7 Fragment AZ-026 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-05-05 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 4 CL CHLORIDE ION × 2 K92 5-[3-(2-azanylethyl)imidazol-4-yl]-4-phenyl-thiophene-2-carboximidamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.60 Å R-free 0.169
6RWH Fragment AZ-007 binding at a primary and secondary binding site of the the p53pT387/14-3-3 sigma complex Deposited 2019-06-05 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) KLB 5-(1~{H}-imidazol-5-yl)-4-phenyl-thiophene-2-carboximidamide × 4 CA CALCIUM ION × 2 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.68 Å R-free 0.227
6RWI Fragment AZ-002 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-06-05 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) KLE 5-phenylthiophene-2-carboximidamide × 2 CA CALCIUM ION × 2 MG MAGNESIUM ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.65 Å R-free 0.204
6RWS Fragment AZ-009 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-06-06 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) KLZ 4-chloranyl-6-(sulfanylmethyl)-1-benzothiophene-2-carboximidamide × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.53 Å R-free 0.200
6RWU Fragment AZ-010 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-06-06 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) KM8 ~{N}-[3-(5-carbamimidoylthiophen-3-yl)phenyl]propanamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.46 Å R-free 0.221
6RX2 Fragment AZ-005 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-06-07 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 6 CA CALCIUM ION × 2 KM2 7-[[(2~{S})-1-azanylpropan-2-yl]amino]-1-benzothiophene-2-carboximidamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.82 Å R-free 0.220
6RZ3 Crystal structure of a complex between the DNA-binding domain of p53 and the carboxyl-terminal conserved region of iASPP Deposited 2019-06-12 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 62–292（231 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；294 K；18% (w/v) polyethylene glycol 3350, 0.18 M tri-sodium citrate
Resolution 4.23 Å R-free 0.292
6S39 Fragment AZ-018 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-06-24 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) K5Z 5-(3-azanylpropyl)-4-phenyl-thiophene-2-carboximidamide × 2 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.88 Å R-free 0.388
6S9Q Fragment AZ-004 binding at a primary and secondary site in a p53pT387/14-3-3 complex Deposited 2019-07-15 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) L1T 4-methyl-5-phenyl-thiophene-2-carboximidamide × 6 CA CALCIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT.
Resolution 1.69 Å R-free 0.226
6SHZ p53 cancer mutant Y220C Deposited 2019-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–311（218 aa） Fragment：DNA-binding domain
Mutation：M133L, V203A, Y220C, N239Y, N268D EDO 1,2-ETHANEDIOL × 2 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT.
Resolution 1.24 Å R-free 0.172
6SHZ p53 cancer mutant Y220C Deposited 2019-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–311（218 aa） Fragment：DNA-binding domain
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT.
Resolution 1.24 Å R-free 0.172
6SI0 p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9323 Deposited 2019-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-binding domain
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 LEK 1-[9-ethyl-7-(1,3-thiazol-4-yl)carbazol-3-yl]-~{N}-methyl-methanamine × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of PK9323 in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.53 Å R-free 0.171
6SI0 p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9323 Deposited 2019-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-binding domain
Mutation：M133L, V203A, Y220C, N239Y, N268D ZN ZINC ION × 1 LEK 1-[9-ethyl-7-(1,3-thiazol-4-yl)carbazol-3-yl]-~{N}-methyl-methanamine × 1 GOL GLYCEROL × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of PK9323 in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.53 Å R-free 0.171
6SI1 p53 cancer mutant Y220H Deposited 2019-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-binding domain
Mutation：M133L, V203A, Y220H, N239Y, N268D ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 1 GOL GLYCEROL × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT.
Resolution 1.44 Å R-free 0.178
6SI1 p53 cancer mutant Y220H Deposited 2019-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-binding domain
Mutation：M133L, V203A, Y220H, N239Y, N268D ZN ZINC ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT.
Resolution 1.44 Å R-free 0.178
6SI2 p53 cancer mutant Y220S Deposited 2019-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-binding domain
Mutation：M133L, V203A, Y220S, N239Y, N268D ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT.
Resolution 1.50 Å R-free 0.178
6SI2 p53 cancer mutant Y220S Deposited 2019-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-binding domain
Mutation：M133L, V203A, Y220S, N239Y, N268D ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT.
Resolution 1.50 Å R-free 0.178
6SI3 p53 cancer mutant Y220S in complex with small-molecule stabilizer PK9301 Deposited 2019-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-binding domain
Mutation：M133L, V203A, Y220S, N239Y, N268D ZN ZINC ION × 1 LEB 1-[7-bromanyl-9-[2,2,2-tris(fluoranyl)ethyl]carbazol-3-yl]-~{N}-methyl-methanamine × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of PK9301 in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.40 Å R-free 0.176
6SI3 p53 cancer mutant Y220S in complex with small-molecule stabilizer PK9301 Deposited 2019-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-binding domain
Mutation：M133L, V203A, Y220S, N239Y, N268D ZN ZINC ION × 1 LEB 1-[7-bromanyl-9-[2,2,2-tris(fluoranyl)ethyl]carbazol-3-yl]-~{N}-methyl-methanamine × 1 EDO 1,2-ETHANEDIOL × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: Saturated solution of PK9301 in 100 mm HEPES, ph 7.2, 10 mM sodium phosphate, ph 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm KCl.
Resolution 1.40 Å R-free 0.176
6SI4 p53 cancer mutant Y220S in complex with small-molecule stabilizer PK9323 Deposited 2019-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-binding domain
Mutation：M133L, V203A, Y220S, N239Y, N268D ZN ZINC ION × 1 LEK 1-[9-ethyl-7-(1,3-thiazol-4-yl)carbazol-3-yl]-~{N}-methyl-methanamine × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT, 2 mM PK9323.
Resolution 1.80 Å R-free 0.225
6SI4 p53 cancer mutant Y220S in complex with small-molecule stabilizer PK9323 Deposited 2019-08-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-binding domain
Mutation：M133L, V203A, Y220S, N239Y, N268D ZN ZINC ION × 1 LEK 1-[9-ethyl-7-(1,3-thiazol-4-yl)carbazol-3-yl]-~{N}-methyl-methanamine × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM sodium phosphate, ph 7.2, 150 mm KCl, 5 mm DTT. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT, 2 mM PK9323.
Resolution 1.80 Å R-free 0.225
6SIN Fragment AZ-020 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-08-10 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) K65 ~{N}-[2-(5-carbamimidoylthiophen-3-yl)phenyl]prop-2-enamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT
Resolution 1.64 Å R-free 0.211
6SIO Fragment AZ-017 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-08-10 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 4 CL CHLORIDE ION × 2 LFQ 5-methyl-4-phenyl-thiophene-2-carboximidamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT
Resolution 1.60 Å R-free 0.195
6SIP Fragment AZ-011 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-08-10 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 4 CL CHLORIDE ION × 2 LFB 7-methoxy-1-benzothiophene-2-carboximidamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT
Resolution 1.60 Å R-free 0.196
6SIQ Fragment AZ-012 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-08-10 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) CL CHLORIDE ION × 2 LF5 4-chloranyl-7-propan-2-yloxy-1-benzothiophene-2-carboximidamide × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT
Resolution 1.60 Å R-free 0.217
6SL6 p53 charged core Deposited 2019-08-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 89–311（223 aa）
Mutation：A138G, L252K, T256R, R267L, N268D GOL GLYCEROL × 2 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；277 K；0.2 M Ammonium citrate tribasic pH 7.0, 20% w/v Polyethylene glycol 3,350
Resolution 1.67 Å R-free 0.180
6SLV Fragment AZ-013 binding at the p53pT387/14-3-3 sigma interface Deposited 2019-08-20 Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain P 382–393（12 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) MG MAGNESIUM ION × 6 CL CHLORIDE ION × 2 LJW 4-(methylamino)-7-propan-2-yloxy-1-benzothiophene-2-carboximidamide × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；277 K；0.1M Hepes, pH7.5, 27%PEG, 5% Glycerol, 0.2M Calcium Chloride, 2mM DTT
Resolution 1.90 Å R-free 0.218
6T58 Structure determination of the transactivation domain of p53 in complex with S100A4 using annexin A2 as a crystallization chaperone Deposited 2019-10-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 17–56（40 aa）
Mutation：A280E,A280E,A280E,A280E GOL GLYCEROL × 2 CA CALCIUM ION × 10 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.12 M Alcohols 0.1 M Sodium HEPES; MOPS (acid) pH7.5 20% v/v Ethylene glycol; 10 % w/v PEG 8000 Morpheus D6
Resolution 3.10 Å R-free 0.272
6T58 Structure determination of the transactivation domain of p53 in complex with S100A4 using annexin A2 as a crystallization chaperone Deposited 2019-10-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain B 17–56（40 aa）
Mutation：A280E,A280E,A280E,A280E GOL GLYCEROL × 2 CA CALCIUM ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.12 M Alcohols 0.1 M Sodium HEPES; MOPS (acid) pH7.5 20% v/v Ethylene glycol; 10 % w/v PEG 8000 Morpheus D6
Resolution 3.10 Å R-free 0.272
6VR1 Complex of HLA-A2, a class I MHC, with a p53 peptide Deposited 2020-02-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain P 168–176（9 aa） Fragment：residues 168-176
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；296 K；15% PEG 8000, 0.1 M Tris-HCl, 0.2 M magnesium chloride
Resolution 2.37 Å R-free 0.274
6VR1 Complex of HLA-A2, a class I MHC, with a p53 peptide Deposited 2020-02-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain Q 168–176（9 aa） Fragment：residues 168-176
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；296 K；15% PEG 8000, 0.1 M Tris-HCl, 0.2 M magnesium chloride
Resolution 2.37 Å R-free 0.274
6VR5 Complex of HLA-A2, a class I MHC, with a p53 peptide Deposited 2020-02-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain P 168–176（9 aa） Fragment：residues 168-176
Mutation：R175H No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；295 K；15% PEG 8000, 0.1 M Tris-HCl, 0.2 M magnesium chloride
Resolution 2.38 Å R-free 0.280
6VR5 Complex of HLA-A2, a class I MHC, with a p53 peptide Deposited 2020-02-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric
Chain Q 168–176（9 aa） Fragment：residues 168-176
Mutation：R175H No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 8；295 K；15% PEG 8000, 0.1 M Tris-HCl, 0.2 M magnesium chloride
Resolution 2.38 Å R-free 0.280
6VRM T cell receptor-p53-HLA-A2 complex Deposited 2020-02-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain P 168–176（9 aa）
Mutation：R175H No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 7；295 K；20% (w/v) polyacrylic acid 5100, 0.1 M HEPES, 20 mM MgCl2
Resolution 2.61 Å R-free 0.275
6VRN T cell receptor-p53-HLA-A2 complex Deposited 2020-02-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain P 168–176（9 aa）
Mutation：R175H No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；pH 6.7；295 K；20% (w/v) PEG 3350, 0.2 M ammonium tartrate dibasic
Resolution 2.46 Å R-free 0.259
6W51 Structure of the antibody fragment H2 in complex with HLA-A*02:01/p53R175H Deposited 2020-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain C 168–176（9 aa）
Mutation：R175H No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；277 K；0.2 M Ammonium chloride, 20% w/v PEG 3350
Resolution 3.53 Å R-free 0.283
6W51 Structure of the antibody fragment H2 in complex with HLA-A*02:01/p53R175H Deposited 2020-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain F 168–176（9 aa）
Mutation：R175H No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；277 K；0.2 M Ammonium chloride, 20% w/v PEG 3350
Resolution 3.53 Å R-free 0.283
6W51 Structure of the antibody fragment H2 in complex with HLA-A*02:01/p53R175H Deposited 2020-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain I 168–176（9 aa）
Mutation：R175H No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；277 K；0.2 M Ammonium chloride, 20% w/v PEG 3350
Resolution 3.53 Å R-free 0.283
6W51 Structure of the antibody fragment H2 in complex with HLA-A*02:01/p53R175H Deposited 2020-03-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain L 168–176（9 aa）
Mutation：R175H PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION；277 K；0.2 M Ammonium chloride, 20% w/v PEG 3350
Resolution 3.53 Å R-free 0.283
6XRE Structure of the p53/RNA polymerase II assembly Deposited 2020-07-12 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 13 PDB declaration: tridecameric
Chain M 1–393（393 aa）
Not recorded MG MAGNESIUM ION × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.9
cryo-EM vitrification conditions Cryogen ETHANE；The assembled p53/Pol II co-complex was applied directly on the grid for 10 sec followed by 5.5 sec of blotting. The sample grid was then washed with 3.5% trehalose in 0.1 M KCl/HEM buffer (20 mM HEPES, 0.2 mM EDTA, 2 mM MgCl2 at pH 7.9) for 10 sec, blotted for 5.5 sec, and finally frozen in liquid ethane.
Resolution 4.60 Å
6ZNC Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human wild-type p53DBD bound to DNA and MQ: wt-DNA-MQ (I) Deposited 2020-07-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Not recorded ZN ZINC ION × 2 QNN (2~{S})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 6 QN8 (2~{R})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；292 K；Protein/DNA ratio 1:2.4, TRIS pH=8.5 100mM, 2.0% Tacsimate(tm) pH=8.0, 16% w/v PEG 3350
Resolution 1.64 Å R-free 0.190
7B46 Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human wild-type p53DBD bound to DNA and MQ: wt-DNA-MQ (P1) Deposited 2020-12-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain B 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain C 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain D 94–293（200 aa） Fragment：p53 human DNA binding domain
Mutation：' Mutation：' Mutation：' Mutation：' ZN ZINC ION × 4 QN8 (2~{R})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 7 ACT ACETATE ION × 1 QNN (2~{S})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 1 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；292 K；Protein/DNA ratio 1:2.4, 0.1M DL-Malic acid pH=7.0, 19% w/v PEG 3350
Resolution 2.02 Å R-free 0.203
7B47 Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273H mutant bound to MQ: R273H-MQ (I) Deposited 2020-12-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain B 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain C 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain D 94–293（200 aa） Fragment：p53 human DNA binding domain
Mutation：R273H Mutation：R273H Mutation：R273H Mutation：R273H ZN ZINC ION × 4 QN8 (2~{R})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 6 QNN (2~{S})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 4 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6.1；292 K；0.1M Li Acetate, 16% w/v PEG 3350
Resolution 1.80 Å R-free 0.202
7B48 Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273H mutant bound to MQ: R273H-MQ (II) Deposited 2020-12-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain B 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain C 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain D 94–293（200 aa） Fragment：p53 human DNA binding domain
Mutation：R273H Mutation：R273H Mutation：R273H Mutation：R273H ZN ZINC ION × 4 QNN (2~{S})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 2 EDO 1,2-ETHANEDIOL × 6 ACT ACETATE ION × 2 PEG DI(HYDROXYETHYL)ETHER × 3 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6.1；292 K；0.2M Li Acetate, 2.0% w/v Agarose, 20% w/v PEG 3350
Resolution 2.05 Å R-free 0.228
7B49 Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273H mutant bound to DNA and MQ: R273H-DNA-MQ Deposited 2020-12-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain B 94–293（200 aa） Fragment：p53 human DNA binding domain
Mutation：R273H Mutation：R273H ZN ZINC ION × 4 QN8 (2~{R})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 4 QNN (2~{S})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 4 FMT FORMIC ACID × 48 ACT ACETATE ION × 4 EDO 1,2-ETHANEDIOL × 8 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6.1；292 K；Protein/DNA ratio 1:1.4, 0.075M Sodium formate, 7.5% w/v PEG 3350
Resolution 1.42 Å R-free 0.229
7B4A Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273H mutant bound to DNA: R273H-DNA Deposited 2020-12-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexamer
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain B 94–293（200 aa） Fragment：p53 human DNA binding domain
Mutation：R273H Mutation：R273H ZN ZINC ION × 4 FMT FORMIC ACID × 4 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6.1；292 K；Protein/DNA ratio 1:1.4, 0.075M Sodium formate, 7.5% w/v PEG 3350
Resolution 1.90 Å R-free 0.254
7B4B Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273C mutant bound to MQ: R273C-MQ (I) Deposited 2020-12-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetramer
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain B 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain C 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain D 94–293（200 aa） Fragment：p53 human DNA binding domain
Mutation：R273C Mutation：R273C Mutation：R273C Mutation：R273C ZN ZINC ION × 4 QN8 (2~{R})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 4 QNN (2~{S})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 6 EDO 1,2-ETHANEDIOL × 4 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6.1；292 K；PROTEIN/DNA RATIO 1:2.4, 0.2M Sodium Fluoride, 20% w/v PEG 3350
Resolution 1.76 Å R-free 0.218
7B4C Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273C mutant bound to MQ: R273C-MQ (II) Deposited 2020-12-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetramer
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain B 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain C 94–293（200 aa） Fragment：p53 human DNA binding domain
Chain D 94–293（200 aa） Fragment：p53 human DNA binding domain
Mutation：R273C Mutation：R273C Mutation：R273C Mutation：R273C ZN ZINC ION × 4 QNN (2~{S})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 6 EDO 1,2-ETHANEDIOL × 4 QN8 (2~{R})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 1 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6.1；292 K；0.2M Sodium Fluoride, 20% w/v PEG 3350
Resolution 1.71 Å R-free 0.182
7B4D Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R273C/S240R double mutant bound to DNA and MQ: R273C/S240R-DNA-MQ Deposited 2020-12-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetramer
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Mutation：R273C S240R ZN ZINC ION × 2 QNN (2~{S})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 6 QN8 (2~{R})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 2 FMT FORMIC ACID × 6 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6.1；292 K；Protein/DNA ratio 1:2.4, 0.2M Sodium formate, 20% w/v PEG 3350
Resolution 1.85 Å R-free 0.204
7B4E Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R282W mutant bound to DNA and MQ: R282W-DNA-MQ Deposited 2020-12-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetramer
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Mutation：R282W ZN ZINC ION × 2 QN8 (2~{R})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 6 QNN (2~{S})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 2 PG4 TETRAETHYLENE GLYCOL × 2 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；pH 6.1；292 K；Protein/DNA ratio 1:1.5, 0.1M Sodium Acetate, 20% w/v PEG 3350
Resolution 1.58 Å R-free 0.201
7B4F Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R282W mutant bound to DNA: R282W-MQ (I) Deposited 2020-12-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetramer
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Mutation：R282W ZN ZINC ION × 2 FMT FORMIC ACID × 4 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；292 K；Protein/DNA ratio 1:1.5, 0.03M Citric acid, 0.07M BIS-TRIS propane pH=7.6, 20% w/v PEG 3350
Resolution 1.78 Å R-free 0.195
7B4G Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human p53DBD-R282W mutant bound to DNA: R282W-MQ (II) Deposited 2020-12-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Mutation：R282W ZN ZINC ION × 2 EDO 1,2-ETHANEDIOL × 8 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；292 K；Protein/DNA ratio 1:1.5, 0.2M Sodium Acetate, 20% w/v PEG 3350
Resolution 1.86 Å R-free 0.205
7B4H Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human wild-type p53DBD bound to DNA and MQ: wt-DNA-MQ (III) Deposited 2020-12-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Not recorded ZN ZINC ION × 2 ACT ACETATE ION × 2 EDO 1,2-ETHANEDIOL × 2 QN8 (2~{R})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 4 QNN (2~{S})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 2 FMT FORMIC ACID × 8 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；292 K；Protein/DNA ratio 1:2.4, 0.1M TRIS pH=8.5, 2% Tacsimate(TM) pH=8.0, 16% w/v PEG 3350
Resolution 1.39 Å R-free 0.200
7B4N Structural basis of reactivation of oncogenic p53 mutants by a small molecule: methylene quinuclidinone (MQ). Human wild-type p53DBD bound to DNA and MQ: wt-DNA-MQ (II) Deposited 2020-12-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 2 PDB declaration: tetrameric
Chain A 94–293（200 aa） Fragment：p53 human DNA binding domain
Not recorded ZN ZINC ION × 2 QN8 (2~{R})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 4 QNN (2~{S})-2-methyl-1-azabicyclo[2.2.2]octan-3-one × 2 FMT FORMIC ACID × 4 X-RAY DIFFRACTION
X-ray crystallization conditions EVAPORATION；292 K；Protein/DNA ratio 1:2.4, 0.1M TRIS pH=8.5, 2% Tacsimate(TM) pH=8.0, 16% w/v PEG 3350
Resolution 1.32 Å R-free 0.166
7BWN Crystal Structure of a Designed Protein Heterocatenane Deposited 2020-04-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain L 326–356（31 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；298.15 K；Bis-Tris, (NH4)2SO4
Resolution 2.40 Å R-free 0.239
7BWN Crystal Structure of a Designed Protein Heterocatenane Deposited 2020-04-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 326–356（31 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；298.15 K；Bis-Tris, (NH4)2SO4
Resolution 2.40 Å R-free 0.239
7BWN Crystal Structure of a Designed Protein Heterocatenane Deposited 2020-04-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 326–356（31 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；298.15 K；Bis-Tris, (NH4)2SO4
Resolution 2.40 Å R-free 0.239
7BWN Crystal Structure of a Designed Protein Heterocatenane Deposited 2020-04-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain G 326–356（31 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；298.15 K；Bis-Tris, (NH4)2SO4
Resolution 2.40 Å R-free 0.239
7BWN Crystal Structure of a Designed Protein Heterocatenane Deposited 2020-04-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 5 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain I 326–356（31 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；298.15 K；Bis-Tris, (NH4)2SO4
Resolution 2.40 Å R-free 0.239
7BWN Crystal Structure of a Designed Protein Heterocatenane Deposited 2020-04-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 6 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain K 326–356（31 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；298.15 K；Bis-Tris, (NH4)2SO4
Resolution 2.40 Å R-free 0.239
7BWN Crystal Structure of a Designed Protein Heterocatenane Deposited 2020-04-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 7 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain N 326–356（31 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；298.15 K；Bis-Tris, (NH4)2SO4
Resolution 2.40 Å R-free 0.239
7BWN Crystal Structure of a Designed Protein Heterocatenane Deposited 2020-04-15 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 8 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain P 326–356（31 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；298.15 K；Bis-Tris, (NH4)2SO4
Resolution 2.40 Å R-free 0.239
7DHY Arsenic-bound p53 DNA-binding domain mutant G245S Deposited 2020-11-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa）
Mutation：G245S ARS ARSENIC × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 M Tris (pH 8.0-8.5), 20% (w/v) PEG 8000, 0.2 M Li2SO4, 2 mM EDTA, and 2 mM As2O3
Resolution 2.15 Å R-free 0.219
7DHY Arsenic-bound p53 DNA-binding domain mutant G245S Deposited 2020-11-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–293（200 aa）
Mutation：G245S ARS ARSENIC × 1 ZN ZINC ION × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 M Tris (pH 8.0-8.5), 20% (w/v) PEG 8000, 0.2 M Li2SO4, 2 mM EDTA, and 2 mM As2O3
Resolution 2.15 Å R-free 0.219
7DHY Arsenic-bound p53 DNA-binding domain mutant G245S Deposited 2020-11-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–293（200 aa）
Mutation：G245S ARS ARSENIC × 1 ZN ZINC ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 M Tris (pH 8.0-8.5), 20% (w/v) PEG 8000, 0.2 M Li2SO4, 2 mM EDTA, and 2 mM As2O3
Resolution 2.15 Å R-free 0.219
7DHY Arsenic-bound p53 DNA-binding domain mutant G245S Deposited 2020-11-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–293（200 aa）
Mutation：G245S ARS ARSENIC × 1 ZN ZINC ION × 1 GOL GLYCEROL × 3 SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 M Tris (pH 8.0-8.5), 20% (w/v) PEG 8000, 0.2 M Li2SO4, 2 mM EDTA, and 2 mM As2O3
Resolution 2.15 Å R-free 0.219
7DHZ Arsenic-bound p53 DNA-binding domain mutant R249S Deposited 2020-11-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa）
Mutation：R249S GOL GLYCEROL × 1 ARS ARSENIC × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；0.1 M Bis-Tris (pH 7) and 22% PEG5000-MME
Resolution 1.74 Å R-free 0.257
7DHZ Arsenic-bound p53 DNA-binding domain mutant R249S Deposited 2020-11-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–293（200 aa）
Mutation：R249S GOL GLYCEROL × 2 ARS ARSENIC × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；291 K；0.1 M Bis-Tris (pH 7) and 22% PEG5000-MME
Resolution 1.74 Å R-free 0.257
7DVD The crystal structure of p53 DNA binding domain and PUMA complex Deposited 2021-01-13 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 92–290（199 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293.15 K；0.1 M Tris (pH 7.0) 20% (w/w) PEG-200 MME
Resolution 2.59 Å R-free 0.318
7DVD The crystal structure of p53 DNA binding domain and PUMA complex Deposited 2021-01-13 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 92–290（199 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293.15 K；0.1 M Tris (pH 7.0) 20% (w/w) PEG-200 MME
Resolution 2.59 Å R-free 0.318
7DVD The crystal structure of p53 DNA binding domain and PUMA complex Deposited 2021-01-13 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 92–290（199 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293.15 K；0.1 M Tris (pH 7.0) 20% (w/w) PEG-200 MME
Resolution 2.59 Å R-free 0.318
7DVD The crystal structure of p53 DNA binding domain and PUMA complex Deposited 2021-01-13 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 92–290（199 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293.15 K；0.1 M Tris (pH 7.0) 20% (w/w) PEG-200 MME
Resolution 2.59 Å R-free 0.318
7EAX Crystal complex of p53-V272M and antimony ion Deposited 2021-03-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 96–289（194 aa）
Mutation：V272M ZN ZINC ION × 1 SB ANTIMONY (III) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1M Tris pH 8.5, 10% w/v PEG3350 and 0.2M Magnesium chloride
Resolution 2.55 Å R-free 0.235
7EAX Crystal complex of p53-V272M and antimony ion Deposited 2021-03-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 96–289（194 aa）
Mutation：V272M ZN ZINC ION × 1 SB ANTIMONY (III) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1M Tris pH 8.5, 10% w/v PEG3350 and 0.2M Magnesium chloride
Resolution 2.55 Å R-free 0.235
7EAX Crystal complex of p53-V272M and antimony ion Deposited 2021-03-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 96–289（194 aa）
Mutation：V272M ZN ZINC ION × 1 SB ANTIMONY (III) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1M Tris pH 8.5, 10% w/v PEG3350 and 0.2M Magnesium chloride
Resolution 2.55 Å R-free 0.235
7EAX Crystal complex of p53-V272M and antimony ion Deposited 2021-03-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 96–289（194 aa）
Mutation：V272M ZN ZINC ION × 1 SB ANTIMONY (III) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1M Tris pH 8.5, 10% w/v PEG3350 and 0.2M Magnesium chloride
Resolution 2.55 Å R-free 0.235
7EDS Human p53 core domain with germline hot spot mutation M133T in complex with the natural PIG3 p53-response element and Arsenic Deposited 2021-03-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Monomer；Protein × 1 PDB declaration: trimeric
Chain A 94–293（200 aa）
Mutation：M133T ARS ARSENIC × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 M Tris pH 8.5-9, 17-19% PEG20000, 0.1 M MgCl2, 2 mM EDTA, 2 mM As2O3
Resolution 1.77 Å R-free 0.227
7EEU Human p53 core domain with hot spot mutation R282W in complex with the natural CDKN1A(p21) p53-response element and Arsenic Deposited 2021-03-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain A 94–293（200 aa）
Chain B 94–293（200 aa）
Chain C 94–293（200 aa）
Chain D 94–293（200 aa）
Mutation：R282W Mutation：R282W Mutation：R282W Mutation：R282W ARS ARSENIC × 4 ZN ZINC ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 M Sodium acetate, 0.1 M HEPES pH 8.0, 10% w/v PEG 4000, 2mM EDTA and 2mM As2O3
Resolution 2.90 Å R-free 0.264
7EEU Human p53 core domain with hot spot mutation R282W in complex with the natural CDKN1A(p21) p53-response element and Arsenic Deposited 2021-03-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein–DNA Homooligomer；Protein × 4 PDB declaration: hexameric
Chain E 94–293（200 aa）
Chain F 94–293（200 aa）
Chain G 94–293（200 aa）
Chain H 94–293（200 aa）
Mutation：R282W Mutation：R282W Mutation：R282W Mutation：R282W ARS ARSENIC × 4 ZN ZINC ION × 4 PEG DI(HYDROXYETHYL)ETHER × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291 K；0.1 M Sodium acetate, 0.1 M HEPES pH 8.0, 10% w/v PEG 4000, 2mM EDTA and 2mM As2O3
Resolution 2.90 Å R-free 0.264
7EL4 The crystal structure of p53p peptide fragment in complex with the N-terminal domain of MdmX Deposited 2021-04-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 23–29（7 aa）
Not recorded O4B 1,4,7,10,13,16-HEXAOXACYCLOOCTADECANE × 2 MG MAGNESIUM ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.16；291 K；0.1 M MES pH 6.5, 2 M MgSO4
Resolution 2.11 Å R-free 0.225
7NMI Transactivation domain of p53 in complex with S100P, using annexin A2 as crystallization chaperone Deposited 2021-02-23 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 17–56（40 aa）
Not recorded GOL GLYCEROL × 1 CA CALCIUM ION × 9 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；Morpheus screen (MD) H6 0.1 M Amino acids, 0.1 M Buffer System 2, pH 7.5, 30 % v/v Precipitant Mix 2
Resolution 2.10 Å R-free 0.228
7RM4 Neoantigen p53R175H-specific TCR 6-11 binds to p53R175H-HLA-A2 Deposited 2021-07-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain C 168–176（9 aa）
Mutation：R175H No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；20% (w/v) PEG 3350, 0.1 M Bis-Tris propane (pH 8.5), and 0.2 M Potassium thiocyanate
Resolution 3.33 Å R-free 0.295
7RM4 Neoantigen p53R175H-specific TCR 6-11 binds to p53R175H-HLA-A2 Deposited 2021-07-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain H 168–176（9 aa）
Mutation：R175H No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；20% (w/v) PEG 3350, 0.1 M Bis-Tris propane (pH 8.5), and 0.2 M Potassium thiocyanate
Resolution 3.33 Å R-free 0.295
7RM4 Neoantigen p53R175H-specific TCR 6-11 binds to p53R175H-HLA-A2 Deposited 2021-07-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain M 168–176（9 aa）
Mutation：R175H No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；20% (w/v) PEG 3350, 0.1 M Bis-Tris propane (pH 8.5), and 0.2 M Potassium thiocyanate
Resolution 3.33 Å R-free 0.295
7RM4 Neoantigen p53R175H-specific TCR 6-11 binds to p53R175H-HLA-A2 Deposited 2021-07-26 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric
Chain R 168–176（9 aa）
Mutation：R175H No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；293 K；20% (w/v) PEG 3350, 0.1 M Bis-Tris propane (pH 8.5), and 0.2 M Potassium thiocyanate
Resolution 3.33 Å R-free 0.295
7V97 Arsenic-bound p53 DNA-binding domain mutant V272M Deposited 2021-08-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–293（200 aa）
Not recorded ARS ARSENIC × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；0.1 M Tris pH 8.2, 0.2 M Magnesium chloride, 16% w/v PEG 8000
Resolution 2.02 Å R-free 0.251
7V97 Arsenic-bound p53 DNA-binding domain mutant V272M Deposited 2021-08-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–293（200 aa）
Not recorded ARS ARSENIC × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；0.1 M Tris pH 8.2, 0.2 M Magnesium chloride, 16% w/v PEG 8000
Resolution 2.02 Å R-free 0.251
7V97 Arsenic-bound p53 DNA-binding domain mutant V272M Deposited 2021-08-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–293（200 aa）
Not recorded ARS ARSENIC × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；0.1 M Tris pH 8.2, 0.2 M Magnesium chloride, 16% w/v PEG 8000
Resolution 2.02 Å R-free 0.251
7V97 Arsenic-bound p53 DNA-binding domain mutant V272M Deposited 2021-08-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–293（200 aa）
Not recorded ARS ARSENIC × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；291.15 K；0.1 M Tris pH 8.2, 0.2 M Magnesium chloride, 16% w/v PEG 8000
Resolution 2.02 Å R-free 0.251
7XZX Cryo-EM structure of the nucleosome in complex with p53 DNA-binding domain Deposited 2022-06-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: tetradecameric
Chain K 94–293（200 aa）
Chain L 94–293（200 aa）
Chain M 94–293（200 aa）
Chain N 94–293（200 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.53 Å
7XZZ Cryo-EM structure of the nucleosome in complex with p53 Deposited 2022-06-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: tetradecameric
Chain K 1–393（393 aa）
Chain L 1–393（393 aa）
Chain M 1–393（393 aa）
Chain N 1–393（393 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.07 Å
7YGI Crystal structure of p53 DBD domain in complex with azurin Deposited 2022-07-11 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain A 92–289（198 aa）
Chain B 92–289（198 aa）
Not recorded NA SODIUM ION × 2 ZN ZINC ION × 2 K POTASSIUM ION × 2 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions BATCH MODE；298 K；0.05M Na2HPO4+19.5% PEG3350
Resolution 2.10 Å R-free 0.270
8A31 p53 cancer mutant Y220C in complex with iodophenol-based small-molecule stabilizer JC694 Deposited 2022-06-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-binding domain
Not recorded KV0 4-(3-fluoranylpyrrol-1-yl)-3,5-bis(iodanyl)-2-oxidanyl-benzoic acid × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 5.7 mg/ml protein in 25 mM sodium phosphate, pH 7.2, 150 mm NaCl, 0.5 mM TCEP. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 20 mM compound in 100 mm HEPES, pH 7.2, 10 mM sodium phosphate, pH 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm NaCl.
Resolution 1.46 Å R-free 0.191
8A31 p53 cancer mutant Y220C in complex with iodophenol-based small-molecule stabilizer JC694 Deposited 2022-06-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-binding domain
Not recorded KV0 4-(3-fluoranylpyrrol-1-yl)-3,5-bis(iodanyl)-2-oxidanyl-benzoic acid × 1 ZN ZINC ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 5.7 mg/ml protein in 25 mM sodium phosphate, pH 7.2, 150 mm NaCl, 0.5 mM TCEP. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 20 mM compound in 100 mm HEPES, pH 7.2, 10 mM sodium phosphate, pH 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm NaCl.
Resolution 1.46 Å R-free 0.191
8A32 p53 cancer mutant Y220C in complex with iodophenol-based small-molecule stabilizer JC769 Deposited 2022-06-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-binding domain
Not recorded KVA 4-[3,4-bis(fluoranyl)pyrrol-1-yl]-3,5-bis(iodanyl)-2-oxidanyl-benzoic acid × 1 EDO 1,2-ETHANEDIOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 5.7 mg/ml protein in 25 mM sodium phosphate, pH 7.2, 150 mm NaCl, 0.5 mM TCEP. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 20 mM compound in 100 mm HEPES, pH 7.2, 10 mM sodium phosphate, pH 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm NaCl.
Resolution 1.47 Å R-free 0.193
8A32 p53 cancer mutant Y220C in complex with iodophenol-based small-molecule stabilizer JC769 Deposited 2022-06-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-binding domain
Not recorded KVA 4-[3,4-bis(fluoranyl)pyrrol-1-yl]-3,5-bis(iodanyl)-2-oxidanyl-benzoic acid × 1 ZN ZINC ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 5.7 mg/ml protein in 25 mM sodium phosphate, pH 7.2, 150 mm NaCl, 0.5 mM TCEP. Reservoir buffer: 100 mm HEPES, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mm DTT. Soaking buffer: 20 mM compound in 100 mm HEPES, pH 7.2, 10 mM sodium phosphate, pH 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mm NaCl.
Resolution 1.47 Å R-free 0.193
8A92 p53-Y220C Core Domain in Complex with a Bromo-trifluoro-pyrazole-amine Deposited 2022-06-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：Y220C,M133L,V203A,N239Y,N268D LE9 4-bromanyl-5-(trifluoromethyl)-1H-pyrazol-3-amine × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.15；293 K；100 mM HEPES (pH = 7.15), 19 % PEG4000 and 10 mM DTT
Resolution 1.37 Å R-free 0.183
8A92 p53-Y220C Core Domain in Complex with a Bromo-trifluoro-pyrazole-amine Deposited 2022-06-27 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：Y220C,M133L,V203A,N239Y,N268D LE9 4-bromanyl-5-(trifluoromethyl)-1H-pyrazol-3-amine × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.15；293 K；100 mM HEPES (pH = 7.15), 19 % PEG4000 and 10 mM DTT
Resolution 1.37 Å R-free 0.183
8CG7 Structure of p53 cancer mutant Y220C with arylation at Cys182 and Cys277 Deposited 2023-02-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded ZN ZINC ION × 1 A1IH3 5-iodanyl-2-methylsulfonyl-pyrimidine × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml in 25 mM phosphate buffer, pH 7.2, 0.5 mM TCEP. Crystallization buffer: 19% polyethylene glycol 4000, 100 mM Hepes, pH 7.0. For covalent modification, crystals were soaked for 4 hours in crystallization buffer complemented with 20% glycerol and 30 mM compound before flash freezing in liquid nitrogen.
Resolution 1.53 Å R-free 0.187
8CG7 Structure of p53 cancer mutant Y220C with arylation at Cys182 and Cys277 Deposited 2023-02-03 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded ZN ZINC ION × 1 A1IH3 5-iodanyl-2-methylsulfonyl-pyrimidine × 2 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml in 25 mM phosphate buffer, pH 7.2, 0.5 mM TCEP. Crystallization buffer: 19% polyethylene glycol 4000, 100 mM Hepes, pH 7.0. For covalent modification, crystals were soaked for 4 hours in crystallization buffer complemented with 20% glycerol and 30 mM compound before flash freezing in liquid nitrogen.
Resolution 1.53 Å R-free 0.187
8DC4 Crystal structure of p53 Y220C covalently bound to carbazole KG3 Deposited 2022-06-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：Y220C ZN ZINC ION × 1 R3R 9-propanoyl-9H-carbazole-3-carbaldehyde, bound form × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；100 mM HEPES, 2.2M MgSO4
Resolution 2.40 Å R-free 0.231
8DC4 Crystal structure of p53 Y220C covalently bound to carbazole KG3 Deposited 2022-06-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：Y220C ZN ZINC ION × 1 R3R 9-propanoyl-9H-carbazole-3-carbaldehyde, bound form × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；100 mM HEPES, 2.2M MgSO4
Resolution 2.40 Å R-free 0.231
8DC4 Crystal structure of p53 Y220C covalently bound to carbazole KG3 Deposited 2022-06-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–312（219 aa）
Mutation：Y220C ZN ZINC ION × 1 R3R 9-propanoyl-9H-carbazole-3-carbaldehyde, bound form × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；100 mM HEPES, 2.2M MgSO4
Resolution 2.40 Å R-free 0.231
8DC4 Crystal structure of p53 Y220C covalently bound to carbazole KG3 Deposited 2022-06-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–312（219 aa）
Mutation：Y220C ZN ZINC ION × 1 R3R 9-propanoyl-9H-carbazole-3-carbaldehyde, bound form × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；100 mM HEPES, 2.2M MgSO4
Resolution 2.40 Å R-free 0.231
8DC6 Crystal structure of p53 Y220C covalently bound to indole KG6 Deposited 2022-06-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：Y220C ZN ZINC ION × 1 SO4 SULFATE ION × 5 R4F 1-(2-methylprop-2-enoyl)-1H-indole-3-carbaldehyde, bound form × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；100 mM HEPES, 2.2M MgSO4
Resolution 1.60 Å R-free 0.202
8DC6 Crystal structure of p53 Y220C covalently bound to indole KG6 Deposited 2022-06-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：Y220C ZN ZINC ION × 1 SO4 SULFATE ION × 3 R4F 1-(2-methylprop-2-enoyl)-1H-indole-3-carbaldehyde, bound form × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；100 mM HEPES, 2.2M MgSO4
Resolution 1.60 Å R-free 0.202
8DC6 Crystal structure of p53 Y220C covalently bound to indole KG6 Deposited 2022-06-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 3 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain C 94–312（219 aa）
Mutation：Y220C ZN ZINC ION × 1 SO4 SULFATE ION × 2 R4F 1-(2-methylprop-2-enoyl)-1H-indole-3-carbaldehyde, bound form × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；100 mM HEPES, 2.2M MgSO4
Resolution 1.60 Å R-free 0.202
8DC6 Crystal structure of p53 Y220C covalently bound to indole KG6 Deposited 2022-06-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 4 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain D 94–312（219 aa）
Mutation：Y220C ZN ZINC ION × 1 SO4 SULFATE ION × 3 R4F 1-(2-methylprop-2-enoyl)-1H-indole-3-carbaldehyde, bound form × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；100 mM HEPES, 2.2M MgSO4
Resolution 1.60 Å R-free 0.202
8DC7 Crystal structure of p53 Y220C covalently bound to indole KG10 Deposited 2022-06-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded SO4 SULFATE ION × 3 ZN ZINC ION × 1 MG MAGNESIUM ION × 2 R4R 4-[4-(4-methylpiperazin-1-yl)phenyl]-1-(2-methylprop-2-enoyl)-1H-indole-3-carbaldehyde, bound form × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；100 mM HEPES, 2.2M MgSO4
Resolution 1.99 Å R-free 0.193
8DC8 Crystal structure of p53 Y220C covalently bound to azaindole KG13 Deposited 2022-06-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded R50 2-methyl-1-[(4P)-3-methyl-4-(2-methyl-1,2,3,4-tetrahydroisoquinolin-6-yl)-1H-pyrrolo[2,3-c]pyridin-1-yl]prop-2-en-1-one, bound form × 1 SO4 SULFATE ION × 2 ZN ZINC ION × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；298 K；100 mM HEPES, 2.2M MgSO4
Resolution 1.72 Å R-free 0.204
8E7A Crystal structure of the p53 (Y107H) core domain orthorhombic P form Deposited 2022-08-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：S94-T312
Mutation：Y107H ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；291 K；30 % (w/v) PEG 2000 MME, 100 mM potassium thiocyanate
Resolution 1.30 Å R-free 0.174
8E7B Crystal structure of the p53 (Y107H) core domain monoclinic P form Deposited 2022-08-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：S94-T312
Mutation：Y107H ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；28 % (w/v) PEG 2000 MME, 100 mM Bis-Tris
Resolution 2.50 Å R-free 0.279
8E7B Crystal structure of the p53 (Y107H) core domain monoclinic P form Deposited 2022-08-23 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：S94-T312
Mutation：Y107H ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；28 % (w/v) PEG 2000 MME, 100 mM Bis-Tris
Resolution 2.50 Å R-free 0.279
8GCR HPV16 E6-E6AP-p53 complex Deposited 2023-03-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 94–312（219 aa）
Not recorded ZN ZINC ION × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.38 Å
8HLL Crystal structure of p53/BCL2 fusion complex (complex 1) Deposited 2022-11-30 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 95–290（196 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；291 K；PEG 8K 8%-13%, 0.1M HEPES, 0.8% ethylene glycol
Resolution 2.62 Å R-free 0.280
8HLM Crystal structure of p53/BCL2 fusion complex (complex 2) Deposited 2022-11-30 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 95–290（196 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；291 K；0.1 M Imidazole, PEG8K 15-21%
Resolution 2.52 Å R-free 0.290
8HLN Crystal structure of p53/BCL2 fusion complex(complex3) Deposited 2022-11-30 Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 95–290（196 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.8；291 K；0.1 M HEPES, PEG8000 8%-13%, 0.8% ethylene glycol
Resolution 2.35 Å R-free 0.253
8J8N Structure of p53 DNA-binding domain and ZNF568 KRAB domain complex Deposited 2023-05-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 92–292（201 aa） Fragment：DNA binding domain
Chain B 92–292（201 aa） Fragment：DNA binding domain
Chain C 92–292（201 aa） Fragment：DNA binding domain
Chain D 92–292（201 aa） Fragment：DNA binding domain
Not recorded ZN ZINC ION × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.8
cryo-EM vitrification conditions Cryogen NITROGEN
Resolution 9.02 Å
8OXM ATM(Q2971A) activated by oxidative stress in complex with Mg AMP-PNP and p53 peptide Deposited 2023-05-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain E 11–22（12 aa）
Chain F 11–22（12 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
8OXO ATM(Q2971A) dimeric C-terminal region activated by oxidative stress in complex with Mg AMP-PNP and p53 peptide Deposited 2023-05-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric
Chain E 11–22（12 aa）
Chain F 11–22（12 aa）
Not recorded ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER × 2 MG MAGNESIUM ION × 2 ZN ZINC ION × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å
8QWK Structure of p53 cancer mutant Y126C Deposited 2023-10-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 5.5-6.0 mg/ml in 25 mM HEPES (pH 7.5), 300 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 0.7 M sodium citrate and 0.1 M bis-tris-propane (pH 7.0).
Resolution 1.69 Å R-free 0.218
8QWL Structure of p53 cancer mutant Y163C Deposited 2023-10-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 3 MLI MALONATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；Protein solution: 5.5-6.0 mg/ml in 25 mM HEPES (pH 7.5), 200 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 24% PEG 3350 (w/v), 10% ethylene glycol (v/v), 0.2 M sodium malonate (pH 7.0).
Resolution 1.65 Å R-free 0.189
8QWM Structure of p53 cancer mutant Y205C Deposited 2023-10-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded ZN ZINC ION × 1 TLA L(+)-TARTARIC ACID × 1 EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；Protein solution: 5.5-6.0 mg/ml in 25 mM HEPES (pH 7.5), 200 mM NaCl, 0.5 mM TCEP Reservoir buffer: 18% PEG 3350 (w/v), 15% ethylene glycol (v/v), 0.2 M Na/K tartrate.
Resolution 1.54 Å R-free 0.221
8QWM Structure of p53 cancer mutant Y205C Deposited 2023-10-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded ZN ZINC ION × 1 TLA L(+)-TARTARIC ACID × 1 EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；Protein solution: 5.5-6.0 mg/ml in 25 mM HEPES (pH 7.5), 200 mM NaCl, 0.5 mM TCEP Reservoir buffer: 18% PEG 3350 (w/v), 15% ethylene glycol (v/v), 0.2 M Na/K tartrate.
Resolution 1.54 Å R-free 0.221
8QWN Structure of p53 cancer mutant Y220C (hexagonal crystal form) Deposited 2023-10-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 2 MG MAGNESIUM ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 5.5-6.0 mg/ml in 25 mM HEPES (pH 7.5), 200 mM NaCl, 0.5 mM TCEP Reservoir buffer: 20% w/v PEG 8000 (w/v), 0.1 M Tris pH 8.5, 0.2 M magnesium chloride hexahydrate.
Resolution 1.44 Å R-free 0.209
8QWO Structure of p53 cancer mutant Y234C Deposited 2023-10-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded ZN ZINC ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 5.5-6.0 mg/ml in 25 mM phosphate (pH 7.5), 150 mM NaCl, 0.5 mM TCEP Reservoir buffer: 19% PEG 4000 (w/v), 0.1 M HEPES (pH 7.0), 5 mM DTT.
Resolution 1.38 Å R-free 0.178
8QWO Structure of p53 cancer mutant Y234C Deposited 2023-10-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded ZN ZINC ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 5.5-6.0 mg/ml in 25 mM phosphate (pH 7.5), 150 mM NaCl, 0.5 mM TCEP Reservoir buffer: 19% PEG 4000 (w/v), 0.1 M HEPES (pH 7.0), 5 mM DTT.
Resolution 1.38 Å R-free 0.178
8QWP Structure of p53 cancer mutant Y236C Deposited 2023-10-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded ZN ZINC ION × 1 TLA L(+)-TARTARIC ACID × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；Protein solution: 5.5-6.0 mg/ml in 25 mM HEPES (pH 7.5), 200 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 19% PEG 3350 (w/v), 5% ethylene glycol (v/v), 0.2 M Na/K tartrate.
Resolution 2.10 Å R-free 0.268
8QWP Structure of p53 cancer mutant Y236C Deposited 2023-10-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded ZN ZINC ION × 1 TLA L(+)-TARTARIC ACID × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；Protein solution: 5.5-6.0 mg/ml in 25 mM HEPES (pH 7.5), 200 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 19% PEG 3350 (w/v), 5% ethylene glycol (v/v), 0.2 M Na/K tartrate.
Resolution 2.10 Å R-free 0.268
8R1F Monomeric E6AP-E6-p53 ternary complex Deposited 2023-11-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric
Chain C 1–393（393 aa）
Not recorded ZN ZINC ION × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.67 Å
8R1G Dimeric ternary structure of E6AP-E6-p53 Deposited 2023-11-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 6 PDB declaration: hexameric
Chain C 1–393（393 aa）
Chain F 1–393（393 aa）
Not recorded ZN ZINC ION × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.99 Å
8RBA p53-Y220C Core Domain Covalently Bound to 2,5,6-trifluoropyridine-3-carbonitrile Soaked at 5 mM Deposited 2023-12-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：M133L, V203A, N239Y, N268D, Y220C YLW 2,5-bis(fluoranyl)pyridine-3-carbonitrile × 1 PEG DI(HYDROXYETHYL)ETHER × 2 EDO 1,2-ETHANEDIOL × 7 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 1.57 Å R-free 0.183
8RBA p53-Y220C Core Domain Covalently Bound to 2,5,6-trifluoropyridine-3-carbonitrile Soaked at 5 mM Deposited 2023-12-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：M133L, V203A, N239Y, N268D, Y220C YLW 2,5-bis(fluoranyl)pyridine-3-carbonitrile × 1 PEG DI(HYDROXYETHYL)ETHER × 2 EDO 1,2-ETHANEDIOL × 5 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZN ZINC ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 1.57 Å R-free 0.183
8RBB p53-Y220C Core Domain Covalently Bound to 2,5,6-trifluoropyridine-3-carbonitrile Soaked at 40 mM Deposited 2023-12-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded YLW 2,5-bis(fluoranyl)pyridine-3-carbonitrile × 5 GOL GLYCEROL × 1 EDO 1,2-ETHANEDIOL × 4 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 1.69 Å R-free 0.207
8RBB p53-Y220C Core Domain Covalently Bound to 2,5,6-trifluoropyridine-3-carbonitrile Soaked at 40 mM Deposited 2023-12-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded YLW 2,5-bis(fluoranyl)pyridine-3-carbonitrile × 4 EDO 1,2-ETHANEDIOL × 3 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 1.69 Å R-free 0.207
8RBC p53-Y220C Core Domain Covalently Bound to 3-amino-5-chloropyrazine-2,6-dicarbonitrile Soaked at 5 mM Deposited 2023-12-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded YM0 3-azanylpyrazine-2,6-dicarbonitrile × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 PEG DI(HYDROXYETHYL)ETHER × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 2.06 Å R-free 0.260
8RBC p53-Y220C Core Domain Covalently Bound to 3-amino-5-chloropyrazine-2,6-dicarbonitrile Soaked at 5 mM Deposited 2023-12-04 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded YM0 3-azanylpyrazine-2,6-dicarbonitrile × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 2.06 Å R-free 0.260
8RCI Human p53 DNA-binding domain bound to DARPin C10 Deposited 2023-12-06 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 94–294（201 aa）
Not recorded EDO 1,2-ETHANEDIOL × 4 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 2.5 mg/ml of p53 DBD-DARPin C10 complex (1:1 ratio) in 50 mM Tris, pH 8, 150 mM NaCl, 0.5 mM TCEP Crystallization buffer: 25 % w/v PEG 3350
Resolution 1.50 Å R-free 0.197
8UQR Crystal structure of the human p53 tetramerization domain Deposited 2023-10-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 326–356（31 aa）
Chain B 326–356（31 aa）
Chain C 326–356（31 aa）
Chain D 326–356（31 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；296 K；15% PEG 1500
Resolution 1.22 Å R-free 0.177
8WD2 The Crystal Structure of p53 from Biortus. Deposited 2023-09-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：M133L,V203A,Y220C,N239Y,N268D PO4 PHOSPHATE ION × 1 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.04M Potassium phosphate monobasic, 16% w/v PEG 8000, 20% v/v Glycerol
Resolution 1.85 Å R-free 0.208
8WD2 The Crystal Structure of p53 from Biortus. Deposited 2023-09-14 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：M133L,V203A,Y220C,N239Y,N268D PO4 PHOSPHATE ION × 1 ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；0.04M Potassium phosphate monobasic, 16% w/v PEG 8000, 20% v/v Glycerol
Resolution 1.85 Å R-free 0.208
8XCB Cocrystal structure of p53 in complex of B20 Deposited 2023-12-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 94–293（200 aa）
Chain B 94–293（200 aa）
Not recorded ZN ZINC ION × 2 GOL GLYCEROL × 1 A1LUZ 2-[2,4-bis(oxidanylidene)-1,3-thiazolidin-5-ylidene]ethanoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1M Tris pH 8.5, 10% w/v PEG3350 and 0.2M Magnesium chloride
Resolution 1.83 Å R-free 0.245
8XCB Cocrystal structure of p53 in complex of B20 Deposited 2023-12-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain C 94–293（200 aa）
Chain D 94–293（200 aa）
Not recorded ZN ZINC ION × 2 GOL GLYCEROL × 2 A1LUZ 2-[2,4-bis(oxidanylidene)-1,3-thiazolidin-5-ylidene]ethanoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；0.1M Tris pH 8.5, 10% w/v PEG3350 and 0.2M Magnesium chloride
Resolution 1.83 Å R-free 0.245
8XCE cocrystal structure of p53 in complex of B23 Deposited 2023-12-08 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 94–293（200 aa）
Chain B 94–293（200 aa）
Chain C 94–293（200 aa）
Chain D 94–293（200 aa）
Not recorded ZN ZINC ION × 4 A1LU0 2-[(2~{Z})-2-(3-ethynylphenyl)imino-4-oxidanylidene-1,3-thiazolidin-5-ylidene]ethanoic acid × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；277 K；0.1M Tris pH 8.5, 10% w/v PEG3350 and 0.2M Magnesium chloride
Resolution 2.00 Å R-free 0.223
8XP5 The Crystal Structure of p53/BCL-xL fusion complex from Biortus. Deposited 2024-01-03 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 95–292（198 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.05M MgCl2, 0.1M MES pH6.5, 5% PEG 4000, 10% 2-Propanol, 30% w/v D-Sorbito
Resolution 2.55 Å R-free 0.328
8XP5 The Crystal Structure of p53/BCL-xL fusion complex from Biortus. Deposited 2024-01-03 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain B 95–292（198 aa）
Not recorded ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.05M MgCl2, 0.1M MES pH6.5, 5% PEG 4000, 10% 2-Propanol, 30% w/v D-Sorbito
Resolution 2.55 Å R-free 0.328
9BR3 Crystal structure of p53 Y220C mutant in complex with PC-10709 Deposited 2024-05-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：Y220C A1ARO 2-{3-[4-(methanesulfonyl)-2-methoxyanilino]prop-1-yn-1-yl}-N-(1-methylpiperidin-4-yl)-1-(2,2,2-trifluoroethyl)-1H-indol-4-amine × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；289 K；p53, CID 3799, at 6.93mg/ml; Optimization screen PMV1-opt1 e3: 16% PEG 8000, 20% glycerol, 20mM K2HPO4; protein + 1mM BSI 107743; cryo: direct; crystal tracking ID 285723e3, puck tai0-7
Resolution 1.90 Å R-free 0.191
9BR3 Crystal structure of p53 Y220C mutant in complex with PC-10709 Deposited 2024-05-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：Y220C A1ARO 2-{3-[4-(methanesulfonyl)-2-methoxyanilino]prop-1-yn-1-yl}-N-(1-methylpiperidin-4-yl)-1-(2,2,2-trifluoroethyl)-1H-indol-4-amine × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；289 K；p53, CID 3799, at 6.93mg/ml; Optimization screen PMV1-opt1 e3: 16% PEG 8000, 20% glycerol, 20mM K2HPO4; protein + 1mM BSI 107743; cryo: direct; crystal tracking ID 285723e3, puck tai0-7
Resolution 1.90 Å R-free 0.191
9BR4 Crystal structure of p53 Y220C mutant in complex with PC-9859 Deposited 2024-05-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：p53
Not recorded A1ARZ 2-methyl-2-{5-[(3-{4-[(1-methylpiperidin-4-yl)amino]-1-(2,2,2-trifluoroethyl)-1H-indol-2-yl}prop-2-yn-1-yl)amino]pyridin-2-yl}propanenitrile × 1 ZN ZINC ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；289 K；p53, at 6.93mg/ml; Optimization screen PMV1-opt1 e2: 18% PEG 8000, 20% glycerol, 20mM K2HPO4; protein + 1mM compound PC-8959; cryo: direct; crystal tracking ID 272674 e2, puck mqj6-10
Resolution 1.70 Å R-free 0.175
9BR4 Crystal structure of p53 Y220C mutant in complex with PC-9859 Deposited 2024-05-10 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：p53
Not recorded A1ARZ 2-methyl-2-{5-[(3-{4-[(1-methylpiperidin-4-yl)amino]-1-(2,2,2-trifluoroethyl)-1H-indol-2-yl}prop-2-yn-1-yl)amino]pyridin-2-yl}propanenitrile × 1 ZN ZINC ION × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；289 K；p53, at 6.93mg/ml; Optimization screen PMV1-opt1 e2: 18% PEG 8000, 20% glycerol, 20mM K2HPO4; protein + 1mM compound PC-8959; cryo: direct; crystal tracking ID 272674 e2, puck mqj6-10
Resolution 1.70 Å R-free 0.175
9C5S Disulfide-linked, antiparallel p53-derived peptide dimer (CV1) Deposited 2024-06-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 17–30（14 aa）
Chain B 17–30（14 aa）
Chain C 17–30（14 aa）
Chain D 17–30（14 aa）
Mutation：p53-derived Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：p53-derived Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：p53-derived Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：p53-derived Non-standard monomer：Yes (specific site not provided by mmCIF) SO4 SULFATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；291 K；30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulfate, 20% v/v glycerol, 10% w/v PEG4000, 100 mM imidazole/MES monohydrate buffer, pH 6.5
Resolution 1.01 Å R-free 0.202
9CHT Human E3 ligase E6AP in complex with HPV16-E6 and p53 Deposited 2024-07-02 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 1–312（312 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.54 Å
9FZB Human p53 DNA-binding domain bound to DARPin C10-H82R Deposited 2024-07-05 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 94–294（201 aa）
Not recorded EDO 1,2-ETHANEDIOL × 3 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 2.6 mg/ml p53 DBD-DARPin C10-H82R complex in 50 mM HEPES, pH 7.5, 300 mM NaCl, 0.5 mM TCEP. Reservoir solution: 0.1 M Bis-Tris propane, pH 7.5, 0.02 M sodium potassium phosphate, pH 7.5, 20% (w/v) PEG 3350, 10% (v/v) ethylene glycol. Drop volume ratio: 2:1
Resolution 1.44 Å R-free 0.184
9G5H p53-Y220C Core Domain Covalently Bound to 2-chloro-5-cyanopyrazine Soaked at 5 mM Deposited 2024-07-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：Y220C, M133L, V203A, N239Y, N268D A1IIO 5-chloranylpyrazine-2-carbonitrile × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 6 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 1.65 Å R-free 0.206
9G5H p53-Y220C Core Domain Covalently Bound to 2-chloro-5-cyanopyrazine Soaked at 5 mM Deposited 2024-07-17 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：Y220C, M133L, V203A, N239Y, N268D A1IIO 5-chloranylpyrazine-2-carbonitrile × 3 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 3 ZN ZINC ION × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 1.65 Å R-free 0.206
9G6T p53-Y220C Core Domain Covalently Bound to 5-Chloro-6-methylpyrazine-2-carbonitrile Soaked at 5 mM Deposited 2024-07-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 94–312（219 aa）
Chain B 94–312（219 aa）
Mutation：Y220C, M133L, V203A, N239Y, N268D Mutation：Y220C, M133L, V203A, N239Y, N268D A1II4 5-chloranyl-6-methyl-pyrazine-2-carbonitrile × 5 EDO 1,2-ETHANEDIOL × 6 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 3 PEG DI(HYDROXYETHYL)ETHER × 3 GOL GLYCEROL × 3 ZN ZINC ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 1.56 Å R-free 0.199
9G6U p53-Y220C Core Domain Covalently Bound to 3,5-Dichloro-6-Ethylpyrazine-2-carbonitirle Soaked at 5 mM Deposited 2024-07-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：Y220C, M133L, V203A, N239Y, N268D A1II1 3,5-bis(chloranyl)-6-ethyl-pyrazine-2-carbonitrile × 2 PEG DI(HYDROXYETHYL)ETHER × 2 EDO 1,2-ETHANEDIOL × 6 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 1.64 Å R-free 0.229
9G6U p53-Y220C Core Domain Covalently Bound to 3,5-Dichloro-6-Ethylpyrazine-2-carbonitirle Soaked at 5 mM Deposited 2024-07-19 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：Y220C, M133L, V203A, N239Y, N268D A1II1 3,5-bis(chloranyl)-6-ethyl-pyrazine-2-carbonitrile × 3 PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 3 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1 GOL GLYCEROL × 3 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 1.64 Å R-free 0.229
9R04 p53 bound to the nucleosome at position SHL-5.7 (crosslinked sample) Deposited 2025-04-24 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: 14-meric
Chain K 1–393（393 aa）
Chain L 1–393（393 aa）
Chain M 1–393（393 aa）
Chain N 1–393（393 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.20 Å
9R2M p53 bound to nucleosome at position SHL+5.9 (non-crosslinked sample, composite map) Deposited 2025-04-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: 14-meric
Chain K 1–393（393 aa）
Chain L 1–393（393 aa）
Chain M 1–393（393 aa）
Chain N 1–393（393 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.50 Å
9R2P p53 bound to nucleosome at position SHL+5.9 (crosslinked sample) Deposited 2025-04-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: 14-meric
Chain K 1–393（393 aa）
Chain L 1–393（393 aa）
Chain M 1–393（393 aa）
Chain N 1–393（393 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.18 Å
9R2Q p53 bound to nucleosome at position SHL-5.7 (non-crosslinked sample) Deposited 2025-04-30 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein–DNA Heteromer；Protein × 12 PDB declaration: 14-meric
Chain K 1–393（393 aa）
Chain L 1–393（393 aa）
Chain M 1–393（393 aa）
Chain N 1–393（393 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
9S9L Crystal structure of p53 cancer mutant Y220C in complex with rezatapopt precursor Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded ZN ZINC ION × 1 A1JMS ~{N}-[3-[1-ethyl-5-(methylaminomethyl)indol-2-yl]prop-2-ynyl]aniline × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mm sodium phosphate, pH 7.2, 150 mM KCl, 5 mM DTT. Reservoir buffer: 100 mM Hepes, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mM DTT. Soaking buffer: 19 mM compound in 100 mM Hepes, ph 7.2, 10 mM sodium phosphate, pH 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mM KCl.
Resolution 1.38 Å R-free 0.174
9S9L Crystal structure of p53 cancer mutant Y220C in complex with rezatapopt precursor Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded ZN ZINC ION × 1 A1JMS ~{N}-[3-[1-ethyl-5-(methylaminomethyl)indol-2-yl]prop-2-ynyl]aniline × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mm sodium phosphate, pH 7.2, 150 mM KCl, 5 mM DTT. Reservoir buffer: 100 mM Hepes, pH 7.2, 19% (w/v) polyethylene glycol 4000, 5 mM DTT. Soaking buffer: 19 mM compound in 100 mM Hepes, ph 7.2, 10 mM sodium phosphate, pH 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mM KCl.
Resolution 1.38 Å R-free 0.174
9S9M Crystal structure of p53 cancer mutant Y220C in complex with rezatapopt analog 7 Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded A1JMO 2-[3-[(4-dimethylphosphorylphenyl)amino]prop-1-ynyl]-~{N}-(1-methylpiperidin-4-yl)-1-[2,2,2-tris(fluoranyl)ethyl]indol-4-amine × 1 EDO 1,2-ETHANEDIOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；mM Hepes, pH 7.0, 19% (w/v) polyethylene glycol 4000. Soaking buffer: 19 mM compound in 100 mM Hepes, pH 7.2, 10 mM sodium phosphate, pH 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mM KCl.
Resolution 1.83 Å R-free 0.226
9S9M Crystal structure of p53 cancer mutant Y220C in complex with rezatapopt analog 7 Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded A1JMO 2-[3-[(4-dimethylphosphorylphenyl)amino]prop-1-ynyl]-~{N}-(1-methylpiperidin-4-yl)-1-[2,2,2-tris(fluoranyl)ethyl]indol-4-amine × 1 EDO 1,2-ETHANEDIOL × 2 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；mM Hepes, pH 7.0, 19% (w/v) polyethylene glycol 4000. Soaking buffer: 19 mM compound in 100 mM Hepes, pH 7.2, 10 mM sodium phosphate, pH 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mM KCl.
Resolution 1.83 Å R-free 0.226
9S9N Crystal structure of p53 cancer mutant Y220C in complex with rezatapopt analog 8 Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded A1JMP 1-~{tert}-butyl-~{N}-[[3-[4-[[(3~{S},4~{R})-3-fluoranyl-1-methyl-piperidin-4-yl]amino]-1-[2,2,2-tris(fluoranyl)ethyl]indol-2-yl]-1,2,4-oxadiazol-5-yl]methyl]pyrazole-4-carboxamide × 1 EDO 1,2-ETHANEDIOL × 5 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM Hepes, pH 7.5, 150 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 100 mM Hepes, pH 7.0, 19% (w/v) polyethylene glycol 4000. Soaking buffer: 17 mM compound in 100 mM Hepes, pH 7.2, 10 mM sodium phosphate, pH 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mM KCl.
Resolution 1.72 Å R-free 0.207
9S9N Crystal structure of p53 cancer mutant Y220C in complex with rezatapopt analog 8 Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded A1JMP 1-~{tert}-butyl-~{N}-[[3-[4-[[(3~{S},4~{R})-3-fluoranyl-1-methyl-piperidin-4-yl]amino]-1-[2,2,2-tris(fluoranyl)ethyl]indol-2-yl]-1,2,4-oxadiazol-5-yl]methyl]pyrazole-4-carboxamide × 1 EDO 1,2-ETHANEDIOL × 2 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM Hepes, pH 7.5, 150 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 100 mM Hepes, pH 7.0, 19% (w/v) polyethylene glycol 4000. Soaking buffer: 17 mM compound in 100 mM Hepes, pH 7.2, 10 mM sodium phosphate, pH 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mM KCl.
Resolution 1.72 Å R-free 0.207
9S9O Crystal structure of p53 cancer mutant Y220C in complex with rezatapopt Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded ZN ZINC ION × 1 A1JMR 4-[3-[4-[[(3~{S},4~{R})-3-fluoranyl-1-methyl-piperidin-4-yl]amino]-1-[2,2,2-tris(fluoranyl)ethyl]indol-2-yl]prop-2-ynylamino]-3-methoxy-~{N}-methyl-benzamide × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM Hepes, pH 7.5, 150 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 100 mM Hepes, pH 7.0, 19% (w/v) polyethylene glycol 4000. Soaking buffer: 18 mM compound in 100 mM Hepes, pH 7.2, 10 mM sodium phosphate, pH 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mM KCl
Resolution 1.49 Å R-free 0.186
9S9O Crystal structure of p53 cancer mutant Y220C in complex with rezatapopt Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded ZN ZINC ION × 1 A1JMR 4-[3-[4-[[(3~{S},4~{R})-3-fluoranyl-1-methyl-piperidin-4-yl]amino]-1-[2,2,2-tris(fluoranyl)ethyl]indol-2-yl]prop-2-ynylamino]-3-methoxy-~{N}-methyl-benzamide × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml protein in 25 mM Hepes, pH 7.5, 150 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 100 mM Hepes, pH 7.0, 19% (w/v) polyethylene glycol 4000. Soaking buffer: 18 mM compound in 100 mM Hepes, pH 7.2, 10 mM sodium phosphate, pH 7.2, 19% (w/v) polyethylene glycol 4000, 20 % (v/v) glycerol, 150 mM KCl
Resolution 1.49 Å R-free 0.186
9S9P Crystal structure of p53 cancer mutant Y220S in complex with rezatapopt Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa） Fragment：DNA-binding domain
Not recorded ZN ZINC ION × 1 A1JMR 4-[3-[4-[[(3~{S},4~{R})-3-fluoranyl-1-methyl-piperidin-4-yl]amino]-1-[2,2,2-tris(fluoranyl)ethyl]indol-2-yl]prop-2-ynylamino]-3-methoxy-~{N}-methyl-benzamide × 1 EDO 1,2-ETHANEDIOL × 6 NO3 NITRATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml in 25 mM Hepes, pH 7.5, 150 mM NaCl, 0.5 mM TCEP, 1 mM Rezatapopt, 2% DMSO. Reservoir buffer: 0.2 M ammonium nitrate, 20% PEG 3350 (protein:buffer 2:1). Cryo: reservoir buffer supplemented with 23% ethylene glycol.
Resolution 1.40 Å R-free 0.188
9S9P Crystal structure of p53 cancer mutant Y220S in complex with rezatapopt Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa） Fragment：DNA-binding domain
Not recorded ZN ZINC ION × 1 A1JMR 4-[3-[4-[[(3~{S},4~{R})-3-fluoranyl-1-methyl-piperidin-4-yl]amino]-1-[2,2,2-tris(fluoranyl)ethyl]indol-2-yl]prop-2-ynylamino]-3-methoxy-~{N}-methyl-benzamide × 1 EDO 1,2-ETHANEDIOL × 10 NO3 NITRATE ION × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml in 25 mM Hepes, pH 7.5, 150 mM NaCl, 0.5 mM TCEP, 1 mM Rezatapopt, 2% DMSO. Reservoir buffer: 0.2 M ammonium nitrate, 20% PEG 3350 (protein:buffer 2:1). Cryo: reservoir buffer supplemented with 23% ethylene glycol.
Resolution 1.40 Å R-free 0.188
9S9Q Crystal structure of p53 cancer mutant Y220N in complex with rezatapopt Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded ZN ZINC ION × 1 A1JMR 4-[3-[4-[[(3~{S},4~{R})-3-fluoranyl-1-methyl-piperidin-4-yl]amino]-1-[2,2,2-tris(fluoranyl)ethyl]indol-2-yl]prop-2-ynylamino]-3-methoxy-~{N}-methyl-benzamide × 1 EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml in 25 mM Hepes, pH 7.5, 150 mM NaCl, 0.5 mM TCEP, 1 mM Rezatapopt, 2% DMSO. Reservoir buffer: 10% PEG 8000, 8% ethylene glycol, 0.1 M HEPES pH 7.5 (protein:buffer 1:1). Cryo: reservoir buffer supplemented with 23% ethylene glycol.
Resolution 1.87 Å R-free 0.243
9S9Q Crystal structure of p53 cancer mutant Y220N in complex with rezatapopt Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded ZN ZINC ION × 1 A1JMR 4-[3-[4-[[(3~{S},4~{R})-3-fluoranyl-1-methyl-piperidin-4-yl]amino]-1-[2,2,2-tris(fluoranyl)ethyl]indol-2-yl]prop-2-ynylamino]-3-methoxy-~{N}-methyl-benzamide × 1 EDO 1,2-ETHANEDIOL × 5 PEG DI(HYDROXYETHYL)ETHER × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 6 mg/ml in 25 mM Hepes, pH 7.5, 150 mM NaCl, 0.5 mM TCEP, 1 mM Rezatapopt, 2% DMSO. Reservoir buffer: 10% PEG 8000, 8% ethylene glycol, 0.1 M HEPES pH 7.5 (protein:buffer 1:1). Cryo: reservoir buffer supplemented with 23% ethylene glycol.
Resolution 1.87 Å R-free 0.243
9S9R Crystal structure of p53 cancer mutant Y220N Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；22.5% (w/v) BMW PEG smear broad, 0.1 M potassium sodium tartrate, 10% (w/v) ethylene glycol, 0.1 M sodium cacodylate, pH 5.3-5.8
Resolution 1.70 Å R-free 0.229
9S9R Crystal structure of p53 cancer mutant Y220N Deposited 2025-08-06 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；277 K；22.5% (w/v) BMW PEG smear broad, 0.1 M potassium sodium tartrate, 10% (w/v) ethylene glycol, 0.1 M sodium cacodylate, pH 5.3-5.8
Resolution 1.70 Å R-free 0.229
9SPM p53 cancer mutant V143A in complex with DARPin C10 Deposited 2025-09-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 94–294（201 aa）
Not recorded EDO 1,2-ETHANEDIOL × 7 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 0.75 mg/ml p53-DARPin complex in 25 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 20% PEG smear broad, 0.1 M HEPES pH 7.5, 0.2 M ammonium nitrate. Drop volume ratio 1:1.
Resolution 1.71 Å R-free 0.218
9SPN p53 cancer mutant V157F in complex with DARPin C10 Deposited 2025-09-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 94–294（201 aa）
Not recorded EDO 1,2-ETHANEDIOL × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 0.6 mg/ml DARPin-p53 complex in 25 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP. Reservoir solution: 20% PEG3350, 10% ethylene glycol, 0.2 M sodium/potassium phosphate. Drop volume ratio 2:1.
Resolution 1.93 Å R-free 0.223
9SPO p53 cancer mutant Y220C in complex with DARPin C10 Deposited 2025-09-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 94–294（201 aa）
Not recorded EDO 1,2-ETHANEDIOL × 9 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 2.3 mg/ml DARPin-p53 complex in 25 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP. Reservoir solution: 20% PEG3350, 10% ethylene glycol, 0.1 M bis-tris-propane pH 8.5, 0.2 M sodium formate. Drop volume ratio 2:1.
Resolution 1.48 Å R-free 0.182
9SPP p53 cancer mutant Y234C in complex with DARPin C10 Deposited 2025-09-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 94–294（201 aa）
Not recorded EDO 1,2-ETHANEDIOL × 8 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 1.5 mg/ml p53-DARPin complex in 25 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 15% PEG3350, 0.1 M magnesium formate. Drop volume ratio 2:1.
Resolution 1.47 Å R-free 0.192
9SPQ p53 cancer mutant V272M in complex with DARPin C10 Deposited 2025-09-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 94–294（201 aa）
Not recorded ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein solution: 0.9 mg/ml p53-DARPin complex in 25 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 2.4 M sodium malonate. Drop volume ratio 2:1.
Resolution 2.20 Å R-free 0.222
9SPR p53 cancer mutant R282W in complex with DARPin C10 Deposited 2025-09-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 94–294（201 aa）
Not recorded ZN ZINC ION × 1 EDO 1,2-ETHANEDIOL × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein concentration: 1.8 mg/ml in 25 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 25% PEG3350, 0.1M HEPES pH 7.5, 0.2M lithium sulfate. Drop volume ratio 1:1.
Resolution 1.66 Å R-free 0.201
9SPS p53 cancer mutant E285K in complex with DARPin C10-H82R Deposited 2025-09-17 Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 94–294（201 aa）
Not recorded EDO 1,2-ETHANEDIOL × 1 SO4 SULFATE ION × 1 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；Protein concentration p53-DARPin complex: 0.54 mg/ml in 25 mM HEPES pH 7.5, 150 mM NaCl, 0.5 mM TCEP. Reservoir buffer: 25% PEG3350, 0.2 M lithium sulfate monohydrate, 0.1 M Tris pH 8.5. Drop ratio protein vs reservoir buffer: 2:1.
Resolution 1.42 Å R-free 0.177
9SUK p53-R282W Core Domain Covalently Bound to a Vinyl-Sulfone Fragment Deposited 2025-09-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Mutation：M133L, V203A, N239Y, N268D, R282W EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 PEG DI(HYDROXYETHYL)ETHER × 3 A1JQW 3-bromanyl-1-benzothiophene 1,1-dioxide × 1 GOL GLYCEROL × 1 EDO 1,2-ETHANEDIOL × 2 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 1.56 Å R-free 0.206
9SUK p53-R282W Core Domain Covalently Bound to a Vinyl-Sulfone Fragment Deposited 2025-09-29 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Mutation：M133L, V203A, N239Y, N268D, R282W EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 PEG DI(HYDROXYETHYL)ETHER × 1 A1JQW 3-bromanyl-1-benzothiophene 1,1-dioxide × 1 EDO 1,2-ETHANEDIOL × 4 ZN ZINC ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.2；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 1.56 Å R-free 0.206
9SZZ p53-Y220C Core Domain Covalently Bound to a Vinyl-Sulfone Fragment Deposited 2025-10-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 94–312（219 aa）
Not recorded A1JQW 3-bromanyl-1-benzothiophene 1,1-dioxide × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 2 ZN ZINC ION × 1 PGE TRIETHYLENE GLYCOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 1.70 Å R-free 0.213
9SZZ p53-Y220C Core Domain Covalently Bound to a Vinyl-Sulfone Fragment Deposited 2025-10-16 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain B 94–312（219 aa）
Not recorded A1JQW 3-bromanyl-1-benzothiophene 1,1-dioxide × 1 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 ZN ZINC ION × 1 PEG DI(HYDROXYETHYL)ETHER × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；100 mM HEPES (pH = 7.2), 19 % PEG4000 and 10 mM DTT
Resolution 1.70 Å R-free 0.213

291 other PDB entries and 462 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name P53_HUMAN
Isoform —
PDB entities 2
Chains and sequence ranges Author chain B； PDBConstruct 1–18； UniProt 372–389

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 2h2d

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2h2d
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2h2d
Deposition date deposition_date2006-05-18
Structure title titleThe Structural Basis for Sirtuin Substrate Affinity
Keywords keywordsROSSMANN FOLD, SIR2, SIRTUIN, SIR2TM, P53, SIRT1, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier19.89 Å
Radius of gyration Rg (electron density) rg_electron18.75 Å
Forward intensity I(0) i013022100.00
Molecular weight molecular_weight27779.0 kDa
Excluded volume excluded_volume35108 ų
Envelope volume envelope_volume39199 ų
Hydration-shell volume shell_volume17914 ų
Envelope diameter envelope_diameter66.0 Å
Shell Rg shell_rg24.67 Å
Envelope Rg envelope_rg19.06 Å
Shape Rg shape_rg18.69 Å
Total Rg total_rg19.83 Å
Total atoms total_atoms1948
Residues n_residues246
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax64.5 Å
Rg (real space) rg_real19.88 Å
Rg uncertainty (real space) rg_real_error0.43 Å
I(0) (real space) i0_real1.3020e+07
I(0) uncertainty (real space) i0_real_error1.5830e+05
Rg (reciprocal space) rg_reciprocal19.88 Å
I(0) (reciprocal space) i0_reciprocal13020000.0000
Solution quality estimate total_estimate0.8079
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.7 Å
Skewness Skewness skewness0.365
Kurtosis Kurtosis kurtosis-0.303
Angular range angular_range— – 0.4000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2300000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.837; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd2h2da_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.31 — DHS-like NAD/FAD-binding domain
Superfamily Superfamily superfamilyc.31.1 — DHS-like NAD/FAD-binding domain
Family Family familyc.31.1.0 — automated matches

CATH v4.4 (2 domains)

Domain ID domain_id2h2dA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1220 — TPP-binding domain
Domain ID domain_id2h2dA02
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology1600 — SIR2/SIRT2 'Small Domain'
Homologous superfamily homologous superfamily10 — SIR2/SIRT2 'Small Domain'
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8. Citations (1)

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9. Files and Curves (10)