Research workbench
P53 tetramerization domain wild type
Analyse P53 tetramerization domain wild type in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2J0Z
- Type
- protein
- Length
- 124 residues
- Chains
- 4
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellular tumor antigen P53
- UniProt
- P04637
- Pockets
- 1 · best druggability 0.43
Structure
solution nmr · 1 distinct chain · 65% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Cellular tumor antigen P53 | protein | 31 | 65% helix, 16% strand | P04637 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.43 | 0.75 | 26 | empty |
Interfaces
6 interfaces between chains.
- A–B · 1194 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 1112 Ų buried · 13 hydrogen bonds · protein-protein
- B–C · 330 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 323 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 107 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 2J0Z · p53 tetramerization domain wild type · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P04637
- Elsewhere: RCSB PDB 2J0Z · PDBe 2J0Z · UniProt P04637
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