Research workbench
Structural basis of multiple binding capacity of the acrb multidrug efflux pump
Analyse Structural basis of multiple binding capacity of the acrb multidrug efflux pump in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OYE
- Type
- protein
- Length
- 1,006 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acriflavine resistance protein B
- UniProt
- P31224
- Ligands
- CPF
- Pockets
- 11 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acriflavine resistance protein B | protein | 1006 | 47% helix, 16% strand | P31224 |
Ligands and binding sites
- CPF · 1-cyclopropyl-6-fluoro-4-oxo-7-piperazin-1-yl-1,4-dihydroquinoline-3-carboxylic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 550 | 0.82 | 0.87 | 57 | empty |
| 2 | 722 | 0.80 | 0.84 | 75 | empty |
| 3 | 233 | 0.65 | 0.83 | 35 | empty |
| 4 | 266 | 0.58 | 0.78 | 33 | empty |
| 5 | 228 | 0.56 | 0.78 | 31 | empty |
Compared structures
- 1OYE · Structural Basis of Multiple Binding Capacity of the AcrB multidrug Efflux Pump · the same entry in another collection · chain A against A, TM-score 1.00
- P31224 · AlphaFold monomer V2.0 prediction for multidrug efflux pump subunit acrb (P31224) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P31224
- Elsewhere: RCSB PDB 1OYE · PDBe 1OYE · UniProt P31224
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