Research workbench
Asymmetric structure of trimeric acrb from escherichia COLI
Analyse Asymmetric structure of trimeric acrb 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
- 2GIF
- Type
- protein
- Length
- 3,108 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acriflavine resistance protein B
- UniProt
- P31224
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Acriflavine resistance protein B | protein | 1032 | 52% helix, 20% strand | P31224 |
| B | Acriflavine resistance protein B | protein | 1044 | 52% helix, 19% strand | P31224 |
Ligands and binding sites
- FLC · Citrate anion · additive · 2 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 983 | 0.88 | 0.90 | 120 | empty |
| 2 | 740 | 0.86 | 0.90 | 85 | empty |
| 3 | 788 | 0.84 | 0.87 | 96 | empty |
| 4 | 277 | 0.80 | 0.92 | 32 | empty |
| 5 | 261 | 0.79 | 0.92 | 49 | empty |
Interfaces
3 interfaces between chains.
- A–B · 3510 Ų buried · 38 hydrogen bonds · protein-protein
- A–C · 3357 Ų buried · 41 hydrogen bonds · protein-protein
- B–C · 3059 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 2GIF · Asymmetric structure of trimeric AcrB from Escherichia coli · 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 C against A, TM-score 0.99
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 2GIF · PDBe 2GIF · UniProt P31224
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