Research workbench
Crystal structure of the complex of the CAF1M:CAF1 CHAPERONE:SUBUNIT preassembly complex carrying the TYR40ALA mutation in the CAF1M chaperone
Analyse Crystal structure of the complex of the CAF1M:CAF1 CHAPERONE:SUBUNIT… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AYF
- Type
- protein
- Length
- 308 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein CAF1M; F1 capsule antigen
- UniProt
- P26926, P26948
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 2 distinct chains · 3% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein CAF1M | protein | 186 | 3% helix, 56% strand | P26926 |
| B | F1 capsule antigen | protein | 122 | 2% helix, 50% strand | P26948 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 215 | 0.47 | 0.74 | 28 | empty |
| 2 | 116 | 0.43 | 0.77 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 1445 Ų buried · 34 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4AYF · Crystal structure of the complex of the Caf1M:Caf1 chaperone:subunit preassembly complex… · the same entry in another collection · chain A against A, 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 0.98
- P26948 · AlphaFold monomer V2.0 prediction for F1 capsule antigen (P26948) · a predicted model of the same protein · chain B against A, TM-score 0.97
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 4AYF · PDBe 4AYF · UniProt P26926 · UniProt P26948
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.