Research workbench
Crystal structure of the membrane fusion protein cusb from escherichia COLI
Analyse Crystal structure of the membrane fusion protein cusb from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OPO
- Type
- protein
- Length
- 593 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cation efflux system protein cusb
- UniProt
- P77239
- Ligands
- AG
- Pockets
- 7 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cation efflux system protein cusb | protein | 296 | 14% helix, 39% strand | P77239 |
| B | Cation efflux system protein cusb | protein | 297 | 13% helix, 37% strand | P77239 |
Ligands and binding sites
- AG · Silver ion · metal · 2 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 208 | 0.67 | 0.85 | 30 | empty |
| 2 | 116 | 0.66 | 0.89 | 26 | empty |
| 3 | 100 | 0.66 | 0.90 | 25 | empty |
| 4 | 227 | 0.65 | 0.83 | 30 | empty |
| 5 | 127 | 0.40 | 0.74 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 1080 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 3OPO · Crystal structure of the membrane fusion protein CusB from Escherichia coli · the same entry in another collection · chain A against A, TM-score 1.00
- P77239 · AlphaFold monomer V2.0 prediction for cation efflux system protein cusb (P77239) · a predicted model of the same protein · chain A against A, TM-score 0.80
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 P77239
- Elsewhere: RCSB PDB 3OPO · PDBe 3OPO · UniProt P77239
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