MolNFT v1 · #61546 · protein
Crystal structure of the complex of the CAF1M chaperone with the mini- fiber of two CAF1 subunits (CAF1:CAF1), carrying the THR7PHE and ALA9VAL mutations in the gd donor strand
3DOS · Chaperone protein CAF1M: “Crystal structure of the complex of the CAF1M chaperone with the mini- fiber of two CAF1 subunits…”. X-ray diffraction, 9 pockets (best druggability 0.59). MolNFT v1 #61546 on GenesisL1: 3D structure…
- PDB
- 3DOS
- Type
- protein
- Length
- 954 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein CAF1M; F1 capsule antigen
- UniProt
- P26926, P26948
- Pockets
- 9 · best druggability 0.59
Structure
x-ray diffraction · 6 distinct chains · 3% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein CAF1M | protein | 201 | 3% helix, 56% strand | P26926 |
| B | F1 capsule antigen | protein | 147 | 2% helix, 50% strand | P26948 |
| C | F1 capsule antigen | protein | 135 | 2% helix, 47% strand | P26948 |
| D | Chaperone protein CAF1M | protein | 191 | 3% helix, 57% strand | P26926 |
| E | F1 capsule antigen | protein | 149 | 2% helix, 53% strand | P26948 |
| F | F1 capsule antigen | protein | 131 | 2% helix, 49% strand | P26948 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.59 | 0.82 | 41 | empty |
| 2 | 190 | 0.55 | 0.80 | 32 | empty |
| 3 | 296 | 0.55 | 0.76 | 45 | empty |
| 4 | 251 | 0.52 | 0.75 | 23 | empty |
| 5 | 264 | 0.51 | 0.75 | 44 | empty |
Interfaces
8 interfaces between chains.
- D–E · 1749 Ų buried · 40 hydrogen bonds · protein-protein
- A–B · 1669 Ų buried · 38 hydrogen bonds · protein-protein
- B–C · 1263 Ų buried · 32 hydrogen bonds · protein-protein
- E–F · 1224 Ų buried · 30 hydrogen bonds · protein-protein
- B–D · 589 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3DOS · Crystal structure of the complex of the Caf1M chaperone with the mini-fiber of two Caf1… · the same entry in another collection · chain F against F, TM-score 1.00
- P26926 · AlphaFold monomer V2.0 prediction for chaperone protein CAF1M (P26926) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P26948 · AlphaFold monomer V2.0 prediction for F1 capsule antigen (P26948) · a predicted model of the same protein · chain F against A, TM-score 0.96
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
- Every structure of UniProt P26948
- Elsewhere: RCSB PDB 3DOS · PDBe 3DOS · UniProt P26926 · UniProt P26948
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