Research workbench
Crystal structure of acrb double mutant
Analyse Crystal structure of acrb double mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7O3L
- Type
- protein
- Length
- 6,256 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Efflux pump membrane transporter
- UniProt
- E2QH56
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Efflux pump membrane transporter | protein | 1044 | 50% helix, 19% strand | E2QH56 |
| B, C, E, F | Efflux pump membrane transporter | protein | 1042 | 50% helix, 18% strand | E2QH56 |
Ligands and binding sites
- LMT · Dodecyl-beta-D-maltoside · additive · 6 copies · chains A, B, C, D, E, F
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 | 791 | 0.87 | 0.90 | 107 | empty |
| 2 | 747 | 0.87 | 0.90 | 92 | empty |
| 3 | 1199 | 0.86 | 0.87 | 119 | empty |
| 4 | 693 | 0.85 | 0.89 | 78 | empty |
| 5 | 963 | 0.85 | 0.86 | 99 | empty |
Interfaces
8 interfaces between chains.
- A–B · 3539 Ų buried · 47 hydrogen bonds · protein-protein
- D–E · 3463 Ų buried · 41 hydrogen bonds · protein-protein
- A–C · 3450 Ų buried · 39 hydrogen bonds · protein-protein
- D–F · 3419 Ų buried · 33 hydrogen bonds · protein-protein
- E–F · 3049 Ų buried · 39 hydrogen bonds · protein-protein
Compared structures
- 7O3L · Crystal Structure of AcrB Double Mutant · the same entry in another collection · chain A against A, TM-score 1.00
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 E2QH56
- Elsewhere: RCSB PDB 7O3L · PDBe 7O3L · UniProt E2QH56
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