4A63: P73-ASPP2 complex
Crystal structure of the p73-ASPP2 complex at 2.6A resolution. Determined by X-ray diffraction at 2.27 Å resolution. Released 21 Dec 2011.
- Method
- X-ray diffraction
- Resolution
- 2.27 Å
- Organism
- HOMO SAPIENS
- Chains
- 12
- Atoms
- 19,092
- Mol. weight
- 302.62 kDa
- Ligands
- ZN
- Released
- 21 Dec 2011
Explore 4A63 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4A63 contains 96 α-helices and 130 β-strands across 12 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chains A, C, I and K: 5 helices, 14 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 115-117 | 3 | |
| β-strand | 121 | 1 | 1 |
| β-strand | 128-130 | 3 | 2 |
| β-strand | 142-145 | 4 | 1 |
| β-strand | 150-153 | 4 | 1 |
| β-strand | 159-164 | 6 | 2 |
| α-helix | 168-170 | 3 | |
| β-strand | 174-181 | 8 | 1 |
| β-strand | 190 | 1 | 1 |
| α-helix | 195-199 | 5 | |
| β-strand | 215-218 | 4 | 2 |
| β-strand | 224-227 | 4 | 1 |
| β-strand | 234-239 | 6 | 1 |
| α-helix | 242-244 | 3 | |
| β-strand | 250-256 | 7 | 2 |
| β-strand | 271-278 | 8 | 1 |
| β-strand | 284-294 | 11 | 1 |
| α-helix | 298-312 | 15 | |
| β-strand | 315 | 1 | 3 |
Chain B: 13 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 921-923 | 3 | |
| α-helix | 926-936 | 11 | |
| α-helix | 939-945 | 7 | |
| α-helix | 946-948 | 3 | |
| α-helix | 962-968 | 7 | |
| α-helix | 972-981 | 10 | |
| α-helix | 995-1001 | 7 | |
| α-helix | 1005-1013 | 9 | |
| α-helix | 1029-1032 | 4 | |
| α-helix | 1040-1053 | 14 | |
| α-helix | 1058-1060 | 3 | |
| β-strand | 1061-1064 | 4 | 4 |
| β-strand | 1068 | 1 | 5 |
| β-strand | 1075 | 1 | 4 |
| β-strand | 1078 | 1 | 5 |
| β-strand | 1083-1088 | 6 | 4 |
| β-strand | 1097-1102 | 6 | 4 |
| β-strand | 1105-1110 | 6 | 4 |
| α-helix | 1111-1113 | 3 | |
| β-strand | 1114-1115 | 2 | 4 |
| α-helix | 1118-1120 | 3 | |
Chains D, F and L: 10 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 926-936 | 11 | |
| α-helix | 939-945 | 7 | |
| α-helix | 962-968 | 7 | |
| α-helix | 972-981 | 10 | |
| α-helix | 995-1001 | 7 | |
| α-helix | 1005-1013 | 9 | |
| α-helix | 1029-1032 | 4 | |
| α-helix | 1040-1053 | 14 | |
| α-helix | 1058-1060 | 3 | |
| β-strand | 1061-1064 | 4 | 9 |
| β-strand | 1068 | 1 | 10 |
| β-strand | 1075 | 1 | 9 |
| β-strand | 1078 | 1 | 10 |
| β-strand | 1083-1088 | 6 | 9 |
| β-strand | 1097-1102 | 6 | 9 |
| β-strand | 1105-1110 | 6 | 9 |
| α-helix | 1111-1113 | 3 | |
| β-strand | 1114-1115 | 2 | 9 |
Chain E: 5 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 115-117 | 3 | |
| β-strand | 121 | 1 | 11 |
| β-strand | 128-130 | 3 | 12 |
| β-strand | 142-145 | 4 | 11 |
| β-strand | 150-153 | 4 | 11 |
| β-strand | 159-164 | 6 | 12 |
| α-helix | 168-170 | 3 | |
| β-strand | 174-181 | 8 | 11 |
| β-strand | 190 | 1 | 11 |
| α-helix | 195-199 | 5 | |
| β-strand | 215-218 | 4 | 12 |
| β-strand | 224-227 | 4 | 11 |
| β-strand | 234-239 | 6 | 11 |
| α-helix | 242-244 | 3 | |
| β-strand | 250-256 | 7 | 12 |
| β-strand | 271-278 | 8 | 11 |
| β-strand | 284-294 | 11 | 11 |
| α-helix | 298-312 | 15 | |
Chain G: 6 helices, 13 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 115-117 | 3 | |
| β-strand | 121 | 1 | 15 |
| β-strand | 128-130 | 3 | 16 |
| β-strand | 142-145 | 4 | 15 |
| β-strand | 150-153 | 4 | 15 |
| β-strand | 159-164 | 6 | 16 |
| α-helix | 168-170 | 3 | |
| β-strand | 174-181 | 8 | 15 |
| β-strand | 190 | 1 | 15 |
| α-helix | 191 | 1 | |
| α-helix | 195-199 | 5 | |
| β-strand | 215-218 | 4 | 16 |
| β-strand | 224-227 | 4 | 15 |
| β-strand | 234-239 | 6 | 15 |
| α-helix | 242-244 | 3 | |
| β-strand | 250-256 | 7 | 16 |
| β-strand | 271-278 | 8 | 15 |
| β-strand | 284-294 | 11 | 15 |
| α-helix | 298-312 | 15 | |
Chain H: 10 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 926-936 | 11 | |
| α-helix | 939-945 | 7 | |
| α-helix | 962-969 | 8 | |
| α-helix | 972-981 | 10 | |
| α-helix | 995-1001 | 7 | |
| α-helix | 1005-1013 | 9 | |
| α-helix | 1030-1032 | 3 | |
| α-helix | 1040-1053 | 14 | |
| α-helix | 1058-1060 | 3 | |
| β-strand | 1061-1064 | 4 | 17 |
| β-strand | 1068 | 1 | 18 |
| β-strand | 1075 | 1 | 17 |
| β-strand | 1078 | 1 | 18 |
| β-strand | 1083-1088 | 6 | 17 |
| β-strand | 1097-1102 | 6 | 17 |
| β-strand | 1105-1110 | 6 | 17 |
| α-helix | 1111-1113 | 3 | |
| β-strand | 1114-1115 | 2 | 17 |
Chain J: 12 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 926-936 | 11 | |
| α-helix | 939-945 | 7 | |
| α-helix | 946-948 | 3 | |
| α-helix | 962-969 | 8 | |
| α-helix | 972-981 | 10 | |
| α-helix | 995-1001 | 7 | |
| α-helix | 1005-1013 | 9 | |
| α-helix | 1029-1032 | 4 | |
| α-helix | 1040-1053 | 14 | |
| α-helix | 1058-1060 | 3 | |
| β-strand | 1061-1064 | 4 | 20 |
| β-strand | 1068 | 1 | 21 |
| β-strand | 1075 | 1 | 20 |
| β-strand | 1078 | 1 | 21 |
| β-strand | 1083-1088 | 6 | 20 |
| β-strand | 1097-1102 | 6 | 20 |
| β-strand | 1105-1110 | 6 | 20 |
| α-helix | 1111-1113 | 3 | |
| β-strand | 1114-1115 | 2 | 20 |
| α-helix | 1118-1121 | 4 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Tumour protein 73 | A, C, E, G, I, K | protein | 208 | HOMO SAPIENS | O15350 (AlphaFold model) |
| Apoptosis stimulating of P53 protein 2 | B, D, F, H, J, L | protein | 239 | HOMO SAPIENS | Q13625 (AlphaFold model) |
Sequence of entity 1 (A, C, E, G, I, K), FASTA
>4A63_1 TUMOUR PROTEIN 73 (chains A, C, E, G, I, K)
MAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPP
PGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPV
TGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSF
EGRICACPGRDRKADEDHYREAENLYFQ
Sequence of entity 2 (B, D, F, H, J, L), FASTA
>4A63_2 APOPTOSIS STIMULATING OF P53 PROTEIN 2 (chains B, D, F, H, J, L)
SMPEITGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEV
DDPSLPNDEGITALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCK
FLVESGAAVFAMTYSDMQTAADKCEEMEEGYTQCSQFLYGVQEKMGIMNKGVIYALWDYE
PQNDDELPMKEGDCMTIIHREDEDEIEWWWARLNDKEGYVPRNLLGLYPRIKPRQRSLA
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| ZN | Zinc ion | Zn | 5 |
Water and common crystallization additives (ACT) are not listed.
Primary citation
Structural Basis for Aspp2 Recognition by the Tumor Suppressor P73. Canning, P., von Delft, F., Bullock, A.N. J Mol Biol (2012) 423:515. DOI 10.1016/J.JMB.2012.08.005 · PubMed
Other PDB entries of the same protein (UniProt O15350 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 5HOB 1.22 Å, p73 homo-tetramerization domain mutant I
- 5HOC 1.36 Å, p73 homo-tetramerization domain mutant II
- 2WQI 1.7 Å, Crystal structure of the human p73 tetramerization domain
- 8P9C 1.76 Å, Crystal structure of p63-p73 heterotetramer (tetramerisation domain) in complex with…
- 9GNB 1.8 Å, Structure of p73 SAM domain in complex with DARPin B9
- 2XWC 1.82 Å, Crystal structure of the DNA binding domain of human TP73 refined at 1.8 A resolution
- 2WQJ 2.0 Å, Crystal structure of a truncated variant of the human p73 tetramerization domain
- 9GLQ 2.1 Å, Crystal structure of p73 tetramerisation domain in complex with darpins 1800
- 8P9E 2.25 Å, Crystal structure of wild type p63-p73 heterotetramer (tetramerisation domain) in…
- 2WTT 2.3 Å, Structure of the human p73 tetramerization domain (crystal form II)
- 1DXS 2.54 Å, Crystal structure of the C-terminal sterile alpha motif (SAM) domain of human p73 alpha…
- 8P9D 2.7 Å, Crystal structure of p63-p73 heterotetramer (tetramerisation domain) in complex with…
Browse structure collections
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