Research workbench
Crystal structures of CusC review conformational changes accompanying folding and transmembrane channel formation
Analyse Crystal structures of CusC review conformational changes accompanying folding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4K7K
- Type
- protein
- Length
- 751 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.53
- Source
- Escherichia coli
- Molecule
- Cation efflux system protein CusC
- UniProt
- P77211
- Pockets
- 11 · best druggability 0.66
Structure
x-ray diffraction · resolution 2.53 · 2 distinct chains · 70% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cation efflux system protein CusC | protein | 380 | 70% helix, 2% strand | P77211 |
| B | Cation efflux system protein CusC | protein | 371 | 70% helix, 2% strand | P77211 |
Pockets
11 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 247 | 0.66 | 0.83 | 37 | empty |
| 2 | 425 | 0.65 | 0.78 | 55 | empty |
| 3 | 231 | 0.64 | 0.82 | 33 | empty |
| 4 | 288 | 0.61 | 0.79 | 44 | empty |
| 5 | 198 | 0.54 | 0.79 | 30 | empty |
Interfaces
1 interface between chains.
- A–B · 938 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4K7K · Crystal structures of cusc review conformational changes accompanying folding and… · the same entry in another collection · chain A against A, TM-score 1.00
- P77211 · AlphaFold monomer V2.0 prediction for cation efflux system protein cusc (P77211) · a predicted model of the same protein · chain B against A, TM-score 0.65
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 P77211
- Elsewhere: RCSB PDB 4K7K · PDBe 4K7K · UniProt P77211
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