MolNFT v1 · #117938 · protein
Apo structure of bacterial efflux pump.
5EN5 · Multidrug efflux pump subunit ACRB,MULTIDRUG efflux pump…: “Apo structure of bacterial efflux pump.”. X-ray diffraction, 20 pockets (best druggability 0.88). MolNFT v1 #117938 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5EN5
- Type
- protein
- Length
- 2,221 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multidrug efflux pump subunit ACRB,MULTIDRUG efflux pump subunit acrb; Darpin
- UniProt
- P31224
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 6 distinct chains · 37% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multidrug efflux pump subunit ACRB,MULTIDRUG efflux pump subunit acrb | protein | 580 | 33% helix, 36% strand | P31224 |
| B | Multidrug efflux pump subunit ACRB,MULTIDRUG efflux pump subunit acrb | protein | 578 | 34% helix, 35% strand | P31224 |
| C | Multidrug efflux pump subunit ACRB,MULTIDRUG efflux pump subunit acrb | protein | 584 | 32% helix, 32% strand | P31224 |
| D | Darpin | protein | 161 | 52% helix, 1% strand | — |
| E | Darpin | protein | 156 | 53% helix, 0% strand | — |
| F | Darpin | protein | 162 | 52% helix, 0% strand | — |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 904 | 0.88 | 0.91 | 124 | empty |
| 2 | 963 | 0.87 | 0.89 | 109 | empty |
| 3 | 1135 | 0.85 | 0.86 | 104 | empty |
| 4 | 832 | 0.84 | 0.86 | 87 | empty |
| 5 | 1029 | 0.83 | 0.84 | 97 | empty |
Interfaces
9 interfaces between chains.
- B–C · 3114 Ų buried · 41 hydrogen bonds · protein-protein
- A–B · 3017 Ų buried · 37 hydrogen bonds · protein-protein
- A–C · 2651 Ų buried · 27 hydrogen bonds · protein-protein
- C–E · 918 Ų buried · 8 hydrogen bonds · protein-protein
- B–D · 862 Ų buried · 9 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 5EN5 · PDBe 5EN5 · UniProt P31224
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