Research workbench
Mutant R280K of human P53
Analyse Mutant R280K of human P53 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FF9
- Type
- protein
- Length
- 772 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellular tumor antigen P53
- UniProt
- P04637
- Ligands
- ZN
- Pockets
- 8 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Cellular tumor antigen P53 | protein | 193 | 10% helix, 34% strand | P04637 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 745 | 0.67 | 0.75 | 66 | empty |
| 2 | 730 | 0.65 | 0.74 | 70 | empty |
| 3 | 159 | 0.44 | 0.75 | 31 | empty |
| 4 | 125 | 0.43 | 0.77 | 29 | empty |
| 5 | 127 | 0.40 | 0.75 | 18 | empty |
Interfaces
5 interfaces between chains.
- A–C · 620 Ų buried · 8 hydrogen bonds · protein-protein
- A–B · 490 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 288 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 140 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 53 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6FF9 · Mutant R280K of human P53 · 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 6FF9 · PDBe 6FF9 · UniProt P04637
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