Current Protein Identity:Q9NP68 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1YC5 Sir2-p53 peptide-nicotinamide Deposited 2004-12-21 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 372–389(18 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) 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
2FEJ Solution structure of human p53 DNA binding domain. Deposited 2005-12-16 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 94–297(204 aa) Fragment:DNA binding domain
Not recorded ZN ZINC ION × 1 SOLUTION NMR
NMR measurement conditions pH 7.1;298 K;Ionic strength (raw mmCIF value) 150 mM;Pressure ambient
NMR sample composition 0.4 mM p53 core U-15N,13C, 2H; 25 mM Tris-HCl pH 7.1; 150 mM NaCl; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.3 mM p53 core U-15N,13C, 2H + reverse ILV 13CH3 ; 25 mM Tris-HCl pH 7.1; 150 mM NaCl; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.3 mM p53 core U-15N,13C, 2H + reverse ILV 13CH3 + reverse Tyr ; 25 mM Tris-HCl pH 7.1; 150 mM NaCl; 100% D2O | 100% D2O
NMR sample composition 0.3 mM p53 core U-15N,13C, 2H + Met and Phe (1H); 25 mM Tris-HCl pH 7.1; 150 mM NaCl; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.3 mM p53 core U-15N,13C, 2H + Met and Arg (1H); 25 mM Tris-HCl pH 7.1; 150 mM NaCl; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.4 mM p53 core U-15N,13C, 2H (50%); 25 mM Tris-HCl pH 7.1; 150 mM NaCl; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.4 mM p53 core N/A; 25 mM Tris-HCl pH 7.1; 150 mM NaCl; 90% H2O, 10% D2O | 90% H2O/10% D2O
NMR sample composition 0.4 mM p53 core N/A; 25 mM Tris-HCl pH 7.1; 150 mM NaCl; 100% D2O | 100% D2O
Resolution not provided
2H1L The Structure of the Oncoprotein SV40 Large T Antigen and p53 Tumor Suppressor Complex Deposited 2006-05-16 Assembly 1 Protein heterocomplex Heteromer;Protein × 12 PDB declaration: dodecameric(12) Consistent with protein count
Chain M 92–292(201 aa) Fragment:DNA Binding Domain, residues 92-292
Chain N 92–292(201 aa) Fragment:DNA Binding Domain, residues 92-292
Chain O 92–292(201 aa) Fragment:DNA Binding Domain, residues 92-292
Chain P 92–292(201 aa) Fragment:DNA Binding Domain, residues 92-292
Chain Q 92–292(201 aa) Fragment:DNA Binding Domain, residues 92-292
Chain R 92–292(201 aa) Fragment:DNA Binding Domain, residues 92-292
Not recorded ZN ZINC ION × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 6.5;298 K;5.4% PEG 4000, 73mM Mops Buffer, 22mM Lithium Sulfate, pH 6.5, VAPOR DIFFUSION, temperature 298K
Resolution 3.16 Å R-free 0.308
2H1L The Structure of the Oncoprotein SV40 Large T Antigen and p53 Tumor Suppressor Complex Deposited 2006-05-16 Assembly 2 Protein heterocomplex Heteromer;Protein × 12 PDB declaration: dodecameric(12) Consistent with protein count
Chain S 92–292(201 aa) Fragment:DNA Binding Domain, residues 92-292
Chain T 92–292(201 aa) Fragment:DNA Binding Domain, residues 92-292
Chain U 92–292(201 aa) Fragment:DNA Binding Domain, residues 92-292
Chain V 92–292(201 aa) Fragment:DNA Binding Domain, residues 92-292
Chain W 92–292(201 aa) Fragment:DNA Binding Domain, residues 92-292
Chain X 92–292(201 aa) Fragment:DNA Binding Domain, residues 92-292
Not recorded ZN ZINC ION × 12 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION;pH 6.5;298 K;5.4% PEG 4000, 73mM Mops Buffer, 22mM Lithium Sulfate, pH 6.5, VAPOR DIFFUSION, temperature 298K
Resolution 3.16 Å R-free 0.308
2H4F Sir2-p53 peptide-NAD+ Deposited 2006-05-24 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain D 372–389(18 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) 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 Assembly 1 Protein heterocomplex Heteromer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain B 372–389(18 aa)
Non-standard monomer:Yes (specific site not provided by mmCIF) 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
2H59 Sir2 H116A-deacetylated p53 peptide-3'-o-acetyl ADP ribose Deposited 2006-05-25 Assembly 1 Protein heterocomplex Heteromer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain D 372–389(18 aa)
Chain E 372–389(18 aa)
Not recorded 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