Research workbench
Structural basis of multidrug transport by the acrb multidrug efflux pump
Analyse Structural basis of multidrug transport by 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
- 1T9W
- Type
- protein
- Length
- 1,016 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acriflavine resistance protein B
- UniProt
- P31224
- Ligands
- NFN
- Pockets
- 10 · best druggability 0.87
Structure
x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acriflavine resistance protein B | protein | 1016 | 47% helix, 15% strand | P31224 |
Ligands and binding sites
- NFN · 6-[[(2-ethoxy-1-naphthalenyl)carbonyl]amino]-3,3-dimethyl-7-oxo-4-thia-1-azabicyclo[3.2.0]heptane-2-carboxylate · ligand · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1055 | 0.87 | 0.88 | 118 | empty |
| 2 | 198 | 0.65 | 0.85 | 32 | empty |
| 3 | 51 | 0.62 | 0.93 | 18 | empty |
| 4 | 284 | 0.58 | 0.77 | 33 | empty |
| 5 | 154 | 0.57 | 0.81 | 27 | empty |
Compared structures
- 1T9W · Structural Basis of Multidrug Transport by 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 1T9W · PDBe 1T9W · UniProt P31224
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