Research workbench
Multidrug efflux pump subunit acrb
Analyse Multidrug efflux pump subunit acrb in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7RR8
- Type
- protein
- Length
- 3,075 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multidrug efflux pump subunit acrb
- UniProt
- P31224
- Ligands
- PTY, D12
- Pockets
- 20 · best druggability 0.88
Structure
electron microscopy · 3 distinct chains · 53% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multidrug efflux pump subunit acrb | protein | 1024 | 51% helix, 20% strand | P31224 |
| C | Multidrug efflux pump subunit acrb | protein | 1027 | 53% helix, 17% strand | P31224 |
| B | Multidrug efflux pump subunit acrb | protein | 1024 | 54% helix, 18% strand | P31224 |
Ligands and binding sites
- PTY · Phosphatidylethanolamine · ligand · 13 copies · chains A, C, B
- D12 · Dodecane · ligand · 13 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 | 938 | 0.88 | 0.89 | 128 | empty |
| 2 | 853 | 0.87 | 0.89 | 107 | empty |
| 3 | 566 | 0.82 | 0.88 | 72 | empty |
| 4 | 260 | 0.80 | 0.92 | 33 | empty |
| 5 | 314 | 0.78 | 0.89 | 62 | empty |
Interfaces
3 interfaces between chains.
- A–B · 3547 Ų buried · 35 hydrogen bonds · protein-protein
- A–C · 3249 Ų buried · 35 hydrogen bonds · protein-protein
- C–B · 2930 Ų buried · 30 hydrogen bonds · protein-protein
Compared structures
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 7RR8 · PDBe 7RR8 · UniProt P31224
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