MolNFT v1 · #47227 · protein
CAF1M periplasmic chaperone tetramer
2OS7 · Chaperone protein CAF1M: “CAF1M periplasmic chaperone tetramer”. X-ray diffraction, 13 pockets (best druggability 0.83). MolNFT v1 #47227 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2OS7
- Type
- protein
- Length
- 1,194 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein CAF1M
- UniProt
- P26926
- Pockets
- 13 · best druggability 0.83
Structure
x-ray diffraction · 6 distinct chains · 4% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein CAF1M | protein | 206 | 5% helix, 49% strand | P26926 |
| B | Chaperone protein CAF1M | protein | 196 | 4% helix, 51% strand | P26926 |
| C | Chaperone protein CAF1M | protein | 205 | 5% helix, 53% strand | P26926 |
| D | Chaperone protein CAF1M | protein | 195 | 3% helix, 53% strand | P26926 |
| E | Chaperone protein CAF1M | protein | 202 | 5% helix, 53% strand | P26926 |
| F | Chaperone protein CAF1M | protein | 190 | 3% helix, 55% strand | P26926 |
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1150 | 0.83 | 0.84 | 108 | empty |
| 2 | 987 | 0.82 | 0.83 | 79 | empty |
| 3 | 913 | 0.75 | 0.78 | 70 | empty |
| 4 | 857 | 0.73 | 0.78 | 79 | empty |
| 5 | 136 | 0.65 | 0.88 | 27 | empty |
Interfaces
10 interfaces between chains.
- A–B · 2539 Ų buried · 45 hydrogen bonds · protein-protein
- E–F · 2506 Ų buried · 43 hydrogen bonds · protein-protein
- C–D · 2491 Ų buried · 42 hydrogen bonds · protein-protein
- D–E · 1387 Ų buried · 27 hydrogen bonds · protein-protein
- C–F · 1348 Ų buried · 23 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
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 P26926
- Elsewhere: RCSB PDB 2OS7 · PDBe 2OS7 · UniProt P26926
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