Research workbench
Crystal structure of the complex of the Caf1M:Caf1 chaperone:subunit preassembly complex carrying the KDKDTN insertion at the F1G1 loop region
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
- 4AZ8
- Type
- protein
- Length
- 311 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.65
- Source
- YERSINIA PESTIS
- Molecule
- Chaperone protein CAF1M; F1 capsule antigen
- UniProt
- P26926, P26948
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · resolution 2.65 · 2 distinct chains · 3% helix, 53% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chaperone protein CAF1M | protein | 185 | 4% helix, 56% strand | P26926 |
| B | F1 capsule antigen | protein | 126 | 2% helix, 48% strand | P26948 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 301 | 0.65 | 0.81 | 40 | empty |
Interfaces
1 interface between chains.
- A–B · 1401 Ų buried · 34 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4AZ8 · 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 0.98
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 4AZ8 · PDBe 4AZ8 · UniProt P26926 · UniProt P26948
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