4a63

Crystal structure of the p73-ASPP2 complex at 2.6A resolution

Method: X-RAY DIFFRACTION D_max: 159.5 Å Quality: GOOD

▼

1. Protein Identity and Related Structures Protein Identity & Related Structures

TUMOUR PROTEIN 73

HOMO SAPIENS

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 112–311	Fragment：DNA-BINDING DOMAIN, RESIDUES 1-208	APOPTOSIS STIMULATING OF P53 PROTEIN 2 × 1 （Q13625）	X-RAY DIFFRACTION X-ray crystallization conditions：1.00M NA/KPO4, 0.1M ACETATE PH 4.5	Resolution 2.27 Å R-free 0.244
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain C； UniProt 112–311	Fragment：DNA-BINDING DOMAIN, RESIDUES 1-208	APOPTOSIS STIMULATING OF P53 PROTEIN 2 × 1 （Q13625） ZN ZINC ION × 1 ACT ACETATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：1.00M NA/KPO4, 0.1M ACETATE PH 4.5	Resolution 2.27 Å R-free 0.244
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain E； UniProt 112–311	Fragment：DNA-BINDING DOMAIN, RESIDUES 1-208	APOPTOSIS STIMULATING OF P53 PROTEIN 2 × 1 （Q13625） ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：1.00M NA/KPO4, 0.1M ACETATE PH 4.5	Resolution 2.27 Å R-free 0.244
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain G； UniProt 112–311	Fragment：DNA-BINDING DOMAIN, RESIDUES 1-208	APOPTOSIS STIMULATING OF P53 PROTEIN 2 × 1 （Q13625） ZN ZINC ION × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：1.00M NA/KPO4, 0.1M ACETATE PH 4.5	Resolution 2.27 Å R-free 0.244
5	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain I； UniProt 112–311	Fragment：DNA-BINDING DOMAIN, RESIDUES 1-208	APOPTOSIS STIMULATING OF P53 PROTEIN 2 × 1 （Q13625） ZN ZINC ION × 1 ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：1.00M NA/KPO4, 0.1M ACETATE PH 4.5	Resolution 2.27 Å R-free 0.244
6	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain K； UniProt 112–311	Fragment：DNA-BINDING DOMAIN, RESIDUES 1-208	ZN ZINC ION × 1 ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：1.00M NA/KPO4, 0.1M ACETATE PH 4.5	Resolution 2.27 Å R-free 0.244

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 4A63	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1COK STRUCTURE OF THE C-TERMINAL DOMAIN OF P73 Deposited 1999-05-28	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 439–506（68 aa） Fragment：C-TERMINAL DOMAIN	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6；298 K；Ionic strength (raw mmCIF value) 150mM NACL, 25mM SODIUM PHOSPHATE NMR sample composition 10% WATER/90% D2O	Resolution not provided
1DXS Crystal structure of the C-terminal sterile alpha motif (SAM) domain of human p73 alpha splice variant Deposited 2000-01-15	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 487–564（78 aa） Fragment：C-TERMINAL STERILE ALPHA MOTIF (SAM) DOMAIN	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；290 K；CRYSTALLIZED IN 0.1M TRIS-HCL PH8.5, 2.0M MONO-AMMONIUM DIHYDROGEN PHOSPHATE, AT 290K., pH 8.50	Resolution 2.54 Å R-free 0.346
2KBY The Tetramerization Domain of Human p73 Deposited 2008-12-12	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398 Chain B 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398 Chain C 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398 Chain D 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；303 K；Pressure 1 NMR measurement conditions 303 K；Pressure 1 NMR measurement conditions pH 6.8；303 K；Pressure 1 NMR sample composition 2.5mM [U-13C; U-15N] p73 TD-1, 20mM sodium phosphate-2, 100mM sodium chloride-3, 100% D2O \| 100% D2O NMR sample composition 2.5mM [U-13C; U-15N] p73 TD-4, 20mM sodium phosphate-5, 100mM sodium chloride-6, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 2.5mM [U-15N] p73 TD-7, 20mM sodium phosphate-8, 100mM sodium chloride-9, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 2.5mM [U-15N] p73 TD-10, 2.5mM [U-13C] p73 TD-11, 20mM sodium phosphate-12, 100mM sodium chloride-13, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 2.5mM [U-15N] p73 TD-14, 2.5mM [U-13C] p73 TD-15, 20mM sodium phosphate-16, 100mM sodium chloride-17, 100% D2O \| 100% D2O NMR sample composition 2.5mM [U-10% 13C] p73 TD-18, 20mM sodium phosphate-19, 100mM sodium chloride-20, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 2.5mM [U-13C; U-15N] p73 TD-21, 16.4 Hz Pf1 phage-22, 50mM arginine-23, 50mM glutamate-24, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2MPS Structure of complex of MDM2(3-109) and P73 TAD(10-25) Deposited 2014-06-02	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 10–25（16 aa） Fragment：UNP residues 10-25	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；283 K；Ionic strength (raw mmCIF value) 50；Pressure ambient NMR sample composition 0.9 mM [U-99% 13C; U-99% 15N] E3 Ubiquitin-protein Ligase MDM2-1, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.9 mM [U-99% 13C; U-99% 15N] Tumor protein P73-2, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
2NB1 P63/p73 hetero-tetramerisation domain Deposited 2016-01-19	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain B 351–398（48 aa） Fragment：Tetramerization domain of p73, UNP residues 351-398 Chain D 351–398（48 aa） Fragment：Tetramerization domain of p73, UNP residues 351-398	Mutation：E15K Mutation：E15K	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7；310 K；Ionic strength (raw mmCIF value) 75；Pressure ambient NMR measurement conditions pH 6；310 K；Ionic strength (raw mmCIF value) 5；Pressure ambient NMR sample composition 0.5 mM [U-100% 13C; U-100% 15N] p63 tetramerization domain, 0.5 mM p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.5 mM p63 tetramerization domain, 0.5 mM [U-100% 13C; U-100% 15N] p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.5 mM [U-100% 15N] p63 tetramerization domain, 0.5 mM [U-100% 13C] p63 tetramerization domain, 1 mM p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 1 mM p63 tetramerization domain, 0.5 mM [U-100% 15N] p73 tetramerization domain, 0.5 mM [U-100% 13C] p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 95% H2O/5% D2O \| 95% H2O/5% D2O NMR sample composition 0.5 mM [U-100% 15N] p63 tetramerization domain, 0.5 mM p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 100% D2O \| 100% D2O NMR sample composition 0.5 mM p63 tetramerization domain, 0.5 mM [U-100% 15N] p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 100% D2O \| 100% D2O NMR sample composition 0.5 mM [U-100% 15N] p63 tetramerization domain, 0.5 mM [U-100% 13C] p63 tetramerization domain, 0.5 mM [U-100% 15N] p73 tetramerization domain, 0.5 mM [U-100% 13C] p73 tetramerization domain, 25 mM HEPES, 50 mM sodium chloride, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
2WQI Crystal structure of the human p73 tetramerization domain Deposited 2009-08-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain B 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain C 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain D 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 15 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M SODIUM CITRATE (PH 6.2), 40% PEG 600.	Resolution 1.70 Å R-free 0.254
2WQJ Crystal structure of a truncated variant of the human p73 tetramerization domain Deposited 2009-08-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain G 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain H 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain I 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain J 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain K 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain L 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 10 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M TRIS (PH 8.5), 0.9 M AMMONIUM PHOSPHATE.	Resolution 2.00 Å R-free 0.248
2WQJ Crystal structure of a truncated variant of the human p73 tetramerization domain Deposited 2009-08-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain B 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain C 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain D 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain E 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain F 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 10 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M TRIS (PH 8.5), 0.9 M AMMONIUM PHOSPHATE.	Resolution 2.00 Å R-free 0.248
2WQJ Crystal structure of a truncated variant of the human p73 tetramerization domain Deposited 2009-08-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain S 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain T 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain U 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain V 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain W 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain X 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 10 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M TRIS (PH 8.5), 0.9 M AMMONIUM PHOSPHATE.	Resolution 2.00 Å R-free 0.248
2WQJ Crystal structure of a truncated variant of the human p73 tetramerization domain Deposited 2009-08-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain M 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain N 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain O 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain P 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain Q 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain R 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 10 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M TRIS (PH 8.5), 0.9 M AMMONIUM PHOSPHATE.	Resolution 2.00 Å R-free 0.248
2WQJ Crystal structure of a truncated variant of the human p73 tetramerization domain Deposited 2009-08-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 5 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain 1 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain 2 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain Y 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383 Chain Z 351–383（33 aa） Fragment：TRUNCATED TETRAMERIZATION DOMAIN, RESIDUES 351-383	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 8.5；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 10 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M TRIS (PH 8.5), 0.9 M AMMONIUM PHOSPHATE.	Resolution 2.00 Å R-free 0.248
2WTT Structure of the human p73 tetramerization domain (crystal form II) Deposited 2009-09-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain I 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain J 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain K 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain L 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399	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)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 15 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M SODIUM CITRATE (PH 6.2), 40% PEG 600.	Resolution 2.30 Å R-free 0.287
2WTT Structure of the human p73 tetramerization domain (crystal form II) Deposited 2009-09-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain B 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain C 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain D 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399	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)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 15 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M SODIUM CITRATE (PH 6.2), 40% PEG 600.	Resolution 2.30 Å R-free 0.287
2WTT Structure of the human p73 tetramerization domain (crystal form II) Deposited 2009-09-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain F 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain G 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain H 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399	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)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 15 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M SODIUM CITRATE (PH 6.2), 40% PEG 600.	Resolution 2.30 Å R-free 0.287
2WTT Structure of the human p73 tetramerization domain (crystal form II) Deposited 2009-09-21	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain M 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain N 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain O 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399 Chain P 351–399（49 aa） Fragment：TETRAMERIZATION DOMAIN, RESIDUES 351-399	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)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.2；290 K；SITTING DROP VAPOR DIFFUSION AT 17 DEGREE C. PROTEIN SOLUTION: 15 MG/ML IN 20 MM TRIS (PH 8.5), 50 MM NACL. CRYSTALLIZATION BUFFER: 0.1 M SODIUM CITRATE (PH 6.2), 40% PEG 600.	Resolution 2.30 Å R-free 0.287
2XWC Crystal structure of the DNA binding domain of human TP73 refined at 1.8 A resolution Deposited 2010-11-03	Different construct 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 112–311（200 aa） Fragment：DNA-BINDING DOMAIN, RESIDUES 112-311	Not recorded	ZN ZINC ION × 4 TAM TRIS(HYDROXYETHYL)AMINOMETHANE × 2 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions 1.2M SODIUM POTASSIUM TARTRATE, 0.25% PEG MME 5000, 0.1M TRIS PH 9	Resolution 1.82 Å R-free 0.228
3VD0 structure of p73 DNA binding domain tetramer modulates p73 transactivation Deposited 2012-01-04	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 115–312（198 aa） Fragment：unp residue 115-312 Chain B 115–312（198 aa） Fragment：unp residue 115-312 Chain C 115–312（198 aa） Fragment：unp residue 115-312 Chain D 115–312（198 aa） Fragment：unp residue 115-312	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.1；298 K；0.1M MES, 0.1M Na acetate, pH 6.1, temperature 298.0K	Resolution 2.95 Å R-free 0.254
3VD0 structure of p73 DNA binding domain tetramer modulates p73 transactivation Deposited 2012-01-04	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: octameric	Chain I 115–312（198 aa） Fragment：unp residue 115-312 Chain J 115–312（198 aa） Fragment：unp residue 115-312 Chain K 115–312（198 aa） Fragment：unp residue 115-312 Chain L 115–312（198 aa） Fragment：unp residue 115-312	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.1；298 K；0.1M MES, 0.1M Na acetate, pH 6.1, temperature 298.0K	Resolution 2.95 Å R-free 0.254
3VD1 structure of p73 DNA binding domain tetramer modulates p73 transactivation Deposited 2012-01-04	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 115–312（198 aa） Fragment：unp residue 115-312 Chain B 115–312（198 aa） Fragment：unp residue 115-312 Chain C 115–312（198 aa） Fragment：unp residue 115-312 Chain D 115–312（198 aa） Fragment：unp residue 115-312	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.1；298 K；0.1M MES, 0.1M Na acetate, pH 6.1, temperature 298.0K	Resolution 2.95 Å R-free 0.285
3VD1 structure of p73 DNA binding domain tetramer modulates p73 transactivation Deposited 2012-01-04	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: octameric	Chain I 115–312（198 aa） Fragment：unp residue 115-312 Chain J 115–312（198 aa） Fragment：unp residue 115-312 Chain K 115–312（198 aa） Fragment：unp residue 115-312 Chain L 115–312（198 aa） Fragment：unp residue 115-312	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 6.1；298 K；0.1M MES, 0.1M Na acetate, pH 6.1, temperature 298.0K	Resolution 2.95 Å R-free 0.285
3VD2 structure of p73 DNA binding domain tetramer modulates p73 transactivation Deposited 2012-01-04	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 115–312（198 aa） Fragment：unp residues 115-312 Chain B 115–312（198 aa） Fragment：unp residues 115-312 Chain C 115–312（198 aa） Fragment：unp residues 115-312 Chain D 115–312（198 aa） Fragment：unp residues 115-312	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1M Bis-tris, 0.1M Ammonium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K, pH 6.5	Resolution 4.00 Å R-free 0.284
3VD2 structure of p73 DNA binding domain tetramer modulates p73 transactivation Deposited 2012-01-04	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 I 115–312（198 aa） Fragment：unp residues 115-312 Chain J 115–312（198 aa） Fragment：unp residues 115-312	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.5；298 K；0.1M Bis-tris, 0.1M Ammonium acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K, pH 6.5	Resolution 4.00 Å R-free 0.284
4G82 Crystal Structure of p73 DNA-Binding Domain Tetramer bound to a Full Response-Element Deposited 2012-07-20	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: octameric	Chain A 115–312（198 aa） Fragment：unp residues 115-312 Chain B 115–312（198 aa） Fragment：unp residues 115-312	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 9；298 K；0.1M TRIS, 20% PEG3350 , pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 3.10 Å R-free 0.268
4G83 Crystal Structure of p73 DNA-Binding Domain Tetramer bound to a Full Response-Element Deposited 2012-07-20	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: octameric	Chain A 115–312（198 aa） Chain B 115–312（198 aa）	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；0.1M BTP, 20% PEG3350 , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 4.00 Å R-free 0.307
4GUO structure of p73 DNA binding domain complex with 12 bp DNA Deposited 2012-08-29	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 115–312（198 aa） Fragment：unp residues 115-312 Chain B 115–312（198 aa） Fragment：unp residues 115-312 Chain C 115–312（198 aa） Fragment：unp residues 115-312 Chain D 115–312（198 aa） Fragment：unp residues 115-312	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6；298 K；0.1M MES, 0.1M NA ACETATE, 15-17% PEG 20K, pH 6.0, VAPOR DIFFUSION, temperature 298K	Resolution 3.19 Å R-free 0.270
4GUO structure of p73 DNA binding domain complex with 12 bp DNA Deposited 2012-08-29	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: octameric	Chain I 115–312（198 aa） Fragment：unp residues 115-312 Chain J 115–312（198 aa） Fragment：unp residues 115-312 Chain K 115–312（198 aa） Fragment：unp residues 115-312 Chain L 115–312（198 aa） Fragment：unp residues 115-312	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 6；298 K；0.1M MES, 0.1M NA ACETATE, 15-17% PEG 20K, pH 6.0, VAPOR DIFFUSION, temperature 298K	Resolution 3.19 Å R-free 0.270
4GUQ Structure of mutS139F p73 DNA binding domain complexed with 20BP DNA response element Deposited 2012-08-29	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 115–312（198 aa） Fragment：unp residues 115-312 Chain B 115–312（198 aa） Fragment：unp residues 115-312	Mutation：S139F Mutation：S139F	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；0.1 M Tris, 50-125 mM sodium acetate and 20-24% (w/v) PEG 3350, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 3.70 Å R-free 0.316
5HOB p73 homo-tetramerization domain mutant I Deposited 2016-01-19	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398 Chain B 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398 Chain C 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398 Chain D 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398	Mutation：E363K, K370E, E373R, R390E Mutation：E363K, K370E, E373R, R390E Mutation：E363K, K370E, E373R, R390E Mutation：E363K, K370E, E373R, R390E	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；15% w/v PEG Smear Medium, 0.1 M HEPES pH 7.5, 0.2 M magnesium chloride, 5 % 2-propanol, 10 % ethylene glycol	Resolution 1.22 Å R-free 0.214
5HOB p73 homo-tetramerization domain mutant I Deposited 2016-01-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain E 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398 Chain F 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398 Chain G 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398 Chain H 351–398（48 aa） Fragment：tetramerization domain, UNP residues 351-398	Mutation：E363K, K370E, E373R, R390E Mutation：E363K, K370E, E373R, R390E Mutation：E363K, K370E, E373R, R390E Mutation：E363K, K370E, E373R, R390E	MG MAGNESIUM ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；15% w/v PEG Smear Medium, 0.1 M HEPES pH 7.5, 0.2 M magnesium chloride, 5 % 2-propanol, 10 % ethylene glycol	Resolution 1.22 Å R-free 0.214
5HOC p73 homo-tetramerization domain mutant II Deposited 2016-01-19	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 351–398（48 aa） Fragment：UNP residues 351-398 Chain B 351–398（48 aa） Fragment：UNP residues 351-398	Mutation：E363R, K370E, E373R, R390D Mutation：E363R, K370E, E373R, R390D	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；277 K；2 M Sodium chloride, 0.1 M sodium phosphate, 0.1 M potassium phosphate , 0.1 M HEPES pH 7.5	Resolution 1.36 Å R-free 0.247
5KBD Structural Studies of Transcription Factor p73 DNA Binding Domain Bound to PA26 20-mer Response Element Deposited 2016-06-03	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 115–312（198 aa） Fragment：UNP residues 115-312 Chain B 115–312（198 aa） Fragment：UNP residues 115-312	Not recorded	ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.1 M Tris pH 9.0, 50 mM Sodium Acetate, 16% (w/v) PEG 3350; 2:1 or 4:1 Protein:DNA ratio, 1:1 protein/DNA solution:well solution ratio	Resolution 2.80 Å R-free 0.308
6FGS Solution structure of p300Taz2-p73TA1 Deposited 2018-01-11	Different construct 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 10–31（22 aa）	Not recorded	ZN ZINC ION × 3	SOLUTION NMR NMR measurement conditions pH 6.3；303 K；Ionic strength (raw mmCIF value) 50；Pressure AMBIENT NMR sample composition 700 uM [U-13C; U-15N] Fusion construct of p300 Taz2 and the transactivation domain 1 of p73, 25 mM MES, 50 mM NaCl, 0.5 mM TCEP, 95% H2O/5% D2O \| 95% H2O/5% D2O	Resolution not provided
6IJQ Solution structure of BCL-XL bound to P73-TAD peptide Deposited 2018-10-11	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 10–25（16 aa）	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 6.5；298 K；Ionic strength (raw mmCIF value) 150；Pressure 1 NMR sample composition 1 mM [U-13C; U-15[U-13C; U-15N]N] Bcl-xL, 2 mM p73 peptide, 90% H2O/10% D2O \| 90% H2O/10% D2O NMR sample composition 0.1 mM Bcl-XL, 1 mM p73 peptide, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
7EZJ Crystal structure of p73 DNA binding domain complex bound with 1 bp and 2 bp spacer DNA response elements. Deposited 2021-06-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric	Chain A 115–312（198 aa） Chain B 115–312（198 aa） Chain C 115–312（198 aa） Chain D 115–312（198 aa）	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293.15 K；100 mM MES, pH-6.0, 0.1 M Ammonium acetate, 12% w/v PEg20K	Resolution 2.90 Å R-free 0.306
7EZJ Crystal structure of p73 DNA binding domain complex bound with 1 bp and 2 bp spacer DNA response elements. Deposited 2021-06-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric	Chain I 115–312（198 aa） Chain J 115–312（198 aa） Chain K 115–312（198 aa） Chain L 115–312（198 aa）	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293.15 K；100 mM MES, pH-6.0, 0.1 M Ammonium acetate, 12% w/v PEg20K	Resolution 2.90 Å R-free 0.306
7EZJ Crystal structure of p73 DNA binding domain complex bound with 1 bp and 2 bp spacer DNA response elements. Deposited 2021-06-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 3 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric	Chain a 115–312（198 aa） Chain b 115–312（198 aa） Chain c 115–312（198 aa） Chain d 115–312（198 aa）	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293.15 K；100 mM MES, pH-6.0, 0.1 M Ammonium acetate, 12% w/v PEg20K	Resolution 2.90 Å R-free 0.306
7EZJ Crystal structure of p73 DNA binding domain complex bound with 1 bp and 2 bp spacer DNA response elements. Deposited 2021-06-01	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 4 Protein–DNA Homooligomer；Protein × 4 PDB declaration: octameric	Chain i 115–312（198 aa） Chain j 115–312（198 aa） Chain k 115–312（198 aa） Chain l 115–312（198 aa）	Not recorded	ZN ZINC ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6；293.15 K；100 mM MES, pH-6.0, 0.1 M Ammonium acetate, 12% w/v PEg20K	Resolution 2.90 Å R-free 0.306
8P9C Crystal structure of p63-p73 heterotetramer (tetramerisation domain) in complex with darpin 1810 F11 Deposited 2023-06-05	Different construct 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 351–398（48 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293.15 K；0.2M ammonium acetate, 25% PEG3350, 0.1M HEPES pH 7.5	Resolution 1.76 Å R-free 0.210
8P9D Crystal structure of p63-p73 heterotetramer (tetramerisation domain) in complex with darpin 1810 A2 Deposited 2023-06-05	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric	Chain B 351–398（48 aa） Chain D 351–398（48 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；293.15 K；20% PEG3350, 0.1M bis-tris propane pH 7.0, 0.2M salicylic, sodium salt	Resolution 2.70 Å R-free 0.252
8P9E Crystal structure of wild type p63-p73 heterotetramer (tetramerisation domain) in complex with darpin 1810 F11 Deposited 2023-06-05	Different construct Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: trimeric	Chain B 351–398（48 aa）	Not recorded	GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；293.15 K；0.2M sodium chloride, 25% PEG3350, 0.1M bis-tris pH 6.5	Resolution 2.25 Å R-free 0.250
9GLQ Crystal structure of p73 tetramerisation domain in complex with darpins 1800 Deposited 2024-08-27	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 A 351–398（48 aa） Chain B 351–398（48 aa）	Not recorded	CO COBALT (II) ION × 2 GOL GLYCEROL × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293.15 K；30% PEG2000MME, 0.15M potassium bromide	Resolution 2.10 Å R-free 0.248
9GNB Structure of p73 SAM domain in complex with DARPin B9 Deposited 2024-09-01	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 489–550（62 aa）	Not recorded	SO4 SULFATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 9；293 K；20% PEG6000, 0.1M bicine pH 9.0	Resolution 1.80 Å R-free 0.234

27 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	P73_HUMAN
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 2–201； UniProt 112–311 Author chain C； PDBConstruct 2–201； UniProt 112–311 Author chain E； PDBConstruct 2–201； UniProt 112–311 Author chain G； PDBConstruct 2–201； UniProt 112–311 Author chain I； PDBConstruct 2–201； UniProt 112–311 Author chain K； PDBConstruct 2–201； UniProt 112–311

APOPTOSIS STIMULATING OF P53 PROTEIN 2

HOMO SAPIENS

UniProt Q13625

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 892–1128	Fragment：ANKYRIN AND SH3 DOMAINS, RESIDUES 892-1128	TUMOUR PROTEIN 73 × 1 （O15350）	X-RAY DIFFRACTION X-ray crystallization conditions：1.00M NA/KPO4, 0.1M ACETATE PH 4.5	Resolution 2.27 Å R-free 0.244
2	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain D； UniProt 892–1128	Fragment：ANKYRIN AND SH3 DOMAINS, RESIDUES 892-1128	TUMOUR PROTEIN 73 × 1 （O15350） ZN ZINC ION × 1 ACT ACETATE ION × 3	X-RAY DIFFRACTION X-ray crystallization conditions：1.00M NA/KPO4, 0.1M ACETATE PH 4.5	Resolution 2.27 Å R-free 0.244
3	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain F； UniProt 892–1128	Fragment：ANKYRIN AND SH3 DOMAINS, RESIDUES 892-1128	TUMOUR PROTEIN 73 × 1 （O15350） ZN ZINC ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：1.00M NA/KPO4, 0.1M ACETATE PH 4.5	Resolution 2.27 Å R-free 0.244
4	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain H； UniProt 892–1128	Fragment：ANKYRIN AND SH3 DOMAINS, RESIDUES 892-1128	TUMOUR PROTEIN 73 × 1 （O15350） ZN ZINC ION × 1 ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：1.00M NA/KPO4, 0.1M ACETATE PH 4.5	Resolution 2.27 Å R-free 0.244
5	Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain J； UniProt 892–1128	Fragment：ANKYRIN AND SH3 DOMAINS, RESIDUES 892-1128	TUMOUR PROTEIN 73 × 1 （O15350） ZN ZINC ION × 1 ACT ACETATE ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions：1.00M NA/KPO4, 0.1M ACETATE PH 4.5	Resolution 2.27 Å R-free 0.244
7	Protein monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain L； UniProt 892–1128	Fragment：ANKYRIN AND SH3 DOMAINS, RESIDUES 892-1128	ACT ACETATE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions：1.00M NA/KPO4, 0.1M ACETATE PH 4.5	Resolution 2.27 Å R-free 0.244

Other States of the Same Protein in the Database

Other PDB	Difference from Current Entry 4A63	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1YCS P53-53BP2 COMPLEX Deposited 1996-09-30	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 769–1003（235 aa） Fragment：RESIDUES 327 - 519	Not recorded	ZN ZINC ION × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å R-free 0.286
2UWQ Solution structure of ASPP2 N-terminus Deposited 2007-03-22	Different construct Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–83（83 aa） Fragment：RESIDUES 1-83	Not recorded	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.2；298 K；Ionic strength (raw mmCIF value) 213；Pressure 1.0 NMR measurement conditions pH 7.2；298 K；Ionic strength (raw mmCIF value) 213；Pressure 1.0 NMR sample composition 25MM PHOSPHATE, PH7.2, 150MM NACL, 5MM DTT, 5%D2O	Resolution not provided
4IRV Structure of the Helicobacter pylori CagA Oncogene Bound to the Human Tumor Suppressor Apoptosis-stimulating Protein of p53-2 Deposited 2013-01-15	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain E 726–782（57 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；Crystals were grown by vapor diffusion at 25 degrees C using hanging drops formed from mixing a 2ul of the protein complex with 2ul of an equilibration buffer (21% polyethylene glycol (PEG) molecular weight 4 kDa, 200 mM Li2 SO4 , and 100 mM Tris pH 8.5) and 0.6ul of the Silver Bullets additive 43 (Hampton Research HR2-996-43). Significantly higher quality crystals were obtained from selenomethionine-substituted protein complexes and they were used for the final refinement, VAPOR DIFFUSION, HANGING DROP	Resolution 2.04 Å R-free 0.234
4IRV Structure of the Helicobacter pylori CagA Oncogene Bound to the Human Tumor Suppressor Apoptosis-stimulating Protein of p53-2 Deposited 2013-01-15	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain F 726–782（57 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；Crystals were grown by vapor diffusion at 25 degrees C using hanging drops formed from mixing a 2ul of the protein complex with 2ul of an equilibration buffer (21% polyethylene glycol (PEG) molecular weight 4 kDa, 200 mM Li2 SO4 , and 100 mM Tris pH 8.5) and 0.6ul of the Silver Bullets additive 43 (Hampton Research HR2-996-43). Significantly higher quality crystals were obtained from selenomethionine-substituted protein complexes and they were used for the final refinement, VAPOR DIFFUSION, HANGING DROP	Resolution 2.04 Å R-free 0.234
4IRV Structure of the Helicobacter pylori CagA Oncogene Bound to the Human Tumor Suppressor Apoptosis-stimulating Protein of p53-2 Deposited 2013-01-15	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain G 726–782（57 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；Crystals were grown by vapor diffusion at 25 degrees C using hanging drops formed from mixing a 2ul of the protein complex with 2ul of an equilibration buffer (21% polyethylene glycol (PEG) molecular weight 4 kDa, 200 mM Li2 SO4 , and 100 mM Tris pH 8.5) and 0.6ul of the Silver Bullets additive 43 (Hampton Research HR2-996-43). Significantly higher quality crystals were obtained from selenomethionine-substituted protein complexes and they were used for the final refinement, VAPOR DIFFUSION, HANGING DROP	Resolution 2.04 Å R-free 0.234
4IRV Structure of the Helicobacter pylori CagA Oncogene Bound to the Human Tumor Suppressor Apoptosis-stimulating Protein of p53-2 Deposited 2013-01-15	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain H 726–782（57 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF)	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；Crystals were grown by vapor diffusion at 25 degrees C using hanging drops formed from mixing a 2ul of the protein complex with 2ul of an equilibration buffer (21% polyethylene glycol (PEG) molecular weight 4 kDa, 200 mM Li2 SO4 , and 100 mM Tris pH 8.5) and 0.6ul of the Silver Bullets additive 43 (Hampton Research HR2-996-43). Significantly higher quality crystals were obtained from selenomethionine-substituted protein complexes and they were used for the final refinement, VAPOR DIFFUSION, HANGING DROP	Resolution 2.04 Å R-free 0.234
6GHM Structure of PP1 alpha phosphatase bound to ASPP2 Deposited 2018-05-08	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 926–1134（209 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 8 GOL GLYCEROL × 3 NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID × 3 MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M TRIS pH 8.5 16 % PEG 8000	Resolution 2.15 Å R-free 0.214
6GHM Structure of PP1 alpha phosphatase bound to ASPP2 Deposited 2018-05-08	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 926–1134（209 aa）	Not recorded	EDO 1,2-ETHANEDIOL × 4 GOL GLYCEROL × 1 NHE 2-[N-CYCLOHEXYLAMINO]ETHANE SULFONIC ACID × 3 MN MANGANESE (II) ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；293 K；0.1 M TRIS pH 8.5 16 % PEG 8000	Resolution 2.15 Å R-free 0.214
6HKP Factor Inhibiting HIF (FIH) in complex with zinc, NOG and ASPP2 (970-992) Deposited 2018-09-07	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 S 976–998（23 aa）	Not recorded	SO4 SULFATE ION × 12 GOL GLYCEROL × 10 OGA N-OXALYLGLYCINE × 2 ZN ZINC ION × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；293 K；0.1 M Hepes pH = 7.5, 2.0 M ammonium sulfate, 5.5% PEG400	Resolution 1.90 Å R-free 0.195

5 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ASPP2_HUMAN
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 3–239； UniProt 892–1128 Author chain D； PDBConstruct 3–239； UniProt 892–1128 Author chain F； PDBConstruct 3–239； UniProt 892–1128 Author chain H； PDBConstruct 3–239； UniProt 892–1128 Author chain J； PDBConstruct 3–239； UniProt 892–1128 Author chain L； PDBConstruct 3–239； UniProt 892–1128

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	4a63
Deposition date deposition_date	2011-10-31
Structure title title	Crystal structure of the p73-ASPP2 complex at 2.6A resolution
Keywords keywords	CELL CYCLE, TP53BP2, TUMOUR SUPPRESSOR, ANKYRINS, APOPTOSIS REGULATORY PROTEINS; CELL CYCLE
Experimental Method method	X-RAY DIFFRACTION

▼

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	48.28 Å
Radius of gyration Rg (electron density) rg_electron	47.99 Å
Forward intensity I(0) i0	1052100000.00
Molecular weight molecular_weight	262340.0 kDa
Excluded volume excluded_volume	324860 Å³
Envelope volume envelope_volume	492950 Å³
Hydration-shell volume shell_volume	84626 Å³
Envelope diameter envelope_diameter	158.4 Å
Shell Rg shell_rg	53.83 Å
Envelope Rg envelope_rg	46.34 Å
Shape Rg shape_rg	48.02 Å
Total Rg total_rg	48.13 Å
Total atoms total_atoms	18442
Residues n_residues	2419
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

▼

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	159.5 Å
Rg (real space) rg_real	48.04 Å
Rg uncertainty (real space) rg_real_error	1.20 Å
I(0) (real space) i0_real	1.0520e+09
I(0) uncertainty (real space) i0_real_error	1.9700e+07
Rg (reciprocal space) rg_reciprocal	48.28 Å
I(0) (reciprocal space) i0_reciprocal	1052000000.0000
Solution quality estimate total_estimate	0.8794
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	62.8 Å
Skewness Skewness skewness	0.168
Kurtosis Kurtosis kurtosis	-0.381
Angular range angular_range	— – 0.1650 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	62660000.0000
Real-space data points n_real_points	34
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.982; Smooth: 0.893

▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Description description	TUMOUR PROTEIN 73
Molecular weight formula_weight	23342.6 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,C,E,G,I,K
Atom count atom_count	19119

MAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREAENLYFQ

来源 Source

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	ESCHERICHIA COLI

Entity 2 Entity 2 polymer

Description description	APOPTOSIS STIMULATING OF P53 PROTEIN 2
Molecular weight formula_weight	26951.5 kDa
Source method src_method	man
Copy count entity_count	6

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,D,F,H,J,L

SMPEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGITALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGYTQCSQFLYGVQEKMGIMNKGVIYALWDYEPQNDDELPMKEGDCMTIIHREDEDEIEWWWARLNDKEGYVPRNLLGLYPRIKPRQRSLA

来源 Source

来源生物 organism	HOMO SAPIENS
通用名 common_name	HUMAN
NCBI Class编号 ncbi_taxonomy_id	9606
宿主生物 host_organism	ESCHERICHIA COLI

Entity 3 Entity 3 non-polymer

Description description	ZINC ION
Molecular weight formula_weight	65.4 kDa
Source method src_method	syn
Copy count entity_count	5

Entity 4 Entity 4 non-polymer

Description description	ACETATE ION
Molecular weight formula_weight	59.0 kDa
Source method src_method	syn
Copy count entity_count	9

Entity 5 Entity 5 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	671

▼

7. Fold Classification (SCOP + CATH) 42 domains

SCOP 2.08 (24 domains)

Domain ID domain_id	d4a63a1
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.5 — p53-like transcription factors
Family Family family	b.2.5.2 — p53 DNA-binding domain-like

Domain ID domain_id	d4a63a2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4a63b1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.211 — beta-hairpin-alpha-hairpin repeat
Superfamily Superfamily superfamily	d.211.1 — Ankyrin repeat
Family Family family	d.211.1.1 — Ankyrin repeat

Domain ID domain_id	d4a63b2
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.2 — SH3-domain
Family Family family	b.34.2.0 — automated matches

Domain ID domain_id	d4a63c1
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.5 — p53-like transcription factors
Family Family family	b.2.5.2 — p53 DNA-binding domain-like

Domain ID domain_id	d4a63c2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4a63d1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.211 — beta-hairpin-alpha-hairpin repeat
Superfamily Superfamily superfamily	d.211.1 — Ankyrin repeat
Family Family family	d.211.1.1 — Ankyrin repeat

Domain ID domain_id	d4a63d2
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.2 — SH3-domain
Family Family family	b.34.2.0 — automated matches

Domain ID domain_id	d4a63e1
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.5 — p53-like transcription factors
Family Family family	b.2.5.2 — p53 DNA-binding domain-like

Domain ID domain_id	d4a63e2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4a63f1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.211 — beta-hairpin-alpha-hairpin repeat
Superfamily Superfamily superfamily	d.211.1 — Ankyrin repeat
Family Family family	d.211.1.1 — Ankyrin repeat

Domain ID domain_id	d4a63f2
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.2 — SH3-domain
Family Family family	b.34.2.0 — automated matches

Domain ID domain_id	d4a63g1
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.5 — p53-like transcription factors
Family Family family	b.2.5.2 — p53 DNA-binding domain-like

Domain ID domain_id	d4a63g2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4a63h1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.211 — beta-hairpin-alpha-hairpin repeat
Superfamily Superfamily superfamily	d.211.1 — Ankyrin repeat
Family Family family	d.211.1.1 — Ankyrin repeat

Domain ID domain_id	d4a63h2
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.2 — SH3-domain
Family Family family	b.34.2.0 — automated matches

Domain ID domain_id	d4a63i1
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.5 — p53-like transcription factors
Family Family family	b.2.5.2 — p53 DNA-binding domain-like

Domain ID domain_id	d4a63i2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4a63j1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.211 — beta-hairpin-alpha-hairpin repeat
Superfamily Superfamily superfamily	d.211.1 — Ankyrin repeat
Family Family family	d.211.1.1 — Ankyrin repeat

Domain ID domain_id	d4a63j2
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.2 — SH3-domain
Family Family family	b.34.2.0 — automated matches

Domain ID domain_id	d4a63k1
Class class	b — All beta proteins
Fold Fold fold	b.2 — Common fold of diphtheria toxin/transcription factors/cytochrome f
Superfamily Superfamily superfamily	b.2.5 — p53-like transcription factors
Family Family family	b.2.5.2 — p53 DNA-binding domain-like

Domain ID domain_id	d4a63k2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4a63l1
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.211 — beta-hairpin-alpha-hairpin repeat
Superfamily Superfamily superfamily	d.211.1 — Ankyrin repeat
Family Family family	d.211.1.1 — Ankyrin repeat

Domain ID domain_id	d4a63l2
Class class	b — All beta proteins
Fold Fold fold	b.34 — SH3-like barrel
Superfamily Superfamily superfamily	b.34.2 — SH3-domain
Family Family family	b.34.2.0 — automated matches

CATH v4.4 (18 domains)

Domain ID domain_id	4a63A00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	720 —

Domain ID domain_id	4a63B01
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	20 — Ankyrin repeat-containing domain

Domain ID domain_id	4a63B02
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

Domain ID domain_id	4a63C00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	720 —

Domain ID domain_id	4a63D01
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	20 — Ankyrin repeat-containing domain

Domain ID domain_id	4a63D02
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

Domain ID domain_id	4a63E00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	720 —

Domain ID domain_id	4a63F01
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	20 — Ankyrin repeat-containing domain

Domain ID domain_id	4a63F02
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

Domain ID domain_id	4a63G00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	720 —

Domain ID domain_id	4a63H01
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	20 — Ankyrin repeat-containing domain

Domain ID domain_id	4a63H02
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

Domain ID domain_id	4a63I00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	720 —

Domain ID domain_id	4a63J01
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	20 — Ankyrin repeat-containing domain

Domain ID domain_id	4a63J02
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

Domain ID domain_id	4a63K00
Class class	2 — Mainly Beta
Architecture architecture	60 — Sandwich
Topology topology	40 — Immunoglobulin-like
Homologous superfamily homologous superfamily	720 —

Domain ID domain_id	4a63L01
Class class	1 — Mainly Alpha
Architecture architecture	25 — Alpha Horseshoe
Topology topology	40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily	20 — Ankyrin repeat-containing domain

Domain ID domain_id	4a63L02
Class class	2 — Mainly Beta
Architecture architecture	30 — Roll
Topology topology	30 — SH3 type barrels.
Homologous superfamily homologous superfamily	40 — SH3 Domains

▶

8. Citations (1)

▶

Unit-cell length a length_a	132.810 Å
Unit-cell length b length_b	170.100 Å
Unit-cell length c length_c	177.555 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	91.98 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	24

Space group space_group	I 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.270 Å
Low-resolution limit resolution_low	85.050 Å
R factor r_factor	0.2166
R_work r_work	0.2151
R_free r_free	0.2441

Crystal structure of the p73-ASPP2 complex at 2.6A resolution

1. Protein Identity and Related Structures Protein Identity & Related Structures

TUMOUR PROTEIN 73

State in the Current Structure

Other States of the Same Protein in the Database

APOPTOSIS STIMULATING OF P53 PROTEIN 2

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction

6. Entities and Polymers Entities & Polymers (5)

Entity 1 Entity 1 polymer

Polymer Polymer

来源 Source

Entity 2 Entity 2 polymer

Polymer Polymer

来源 Source

Entity 3 Entity 3 non-polymer

Entity 4 Entity 4 non-polymer

Entity 5 Entity 5 water

7. Fold Classification (SCOP + CATH) 42 domains

SCOP 2.08 (24 domains)

CATH v4.4 (18 domains)

8. Citations (1)

9. Files and Curves (10)

Files (7)

Curves (3)

fit	/app/data/saxs_computation/a6/4a63/4a63.fit
pddf	/app/data/pr_computation/a6/4a63/4a63.pr.out
profile	/app/data/saxs_computation/a6/4a63/4a63.dat