MolNFT v1 · #117961 · protein
Rhodamine bound structure of bacterial efflux pump.
5ENS · Multidrug efflux pump subunit ACRB,MULTIDRUG efflux pump…: “Rhodamine bound structure of bacterial efflux pump.”. X-ray diffraction, 1 ligand (RHQ), 20 pockets (best druggability 0.88). MolNFT v1 #117961 on GenesisL1: 3D structure…
- PDB
- 5ENS
- Type
- protein
- Length
- 2,200 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
- Ligands
- RHQ
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 4 distinct chains · 35% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multidrug efflux pump subunit ACRB,MULTIDRUG efflux pump subunit acrb | protein | 580 | 33% helix, 35% strand | P31224 |
| B | Multidrug efflux pump subunit ACRB,MULTIDRUG efflux pump subunit acrb | protein | 577 | 34% helix, 35% strand | P31224 |
| C | Multidrug efflux pump subunit ACRB,MULTIDRUG efflux pump subunit acrb | protein | 575 | 33% helix, 34% strand | P31224 |
| D, E, F | Darpin | protein | 156 | 53% helix, 0% strand | — |
Ligands and binding sites
- RHQ · Rhodamine 6G · ligand · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1124 | 0.88 | 0.89 | 130 | empty |
| 2 | 972 | 0.87 | 0.89 | 112 | empty |
| 3 | 1059 | 0.85 | 0.86 | 118 | empty |
| 4 | 720 | 0.84 | 0.88 | 89 | RHQ |
| 5 | 971 | 0.83 | 0.84 | 84 | empty |
Interfaces
9 interfaces between chains.
- B–C · 3145 Ų buried · 40 hydrogen bonds · protein-protein
- A–B · 3094 Ų buried · 35 hydrogen bonds · protein-protein
- A–C · 2673 Ų buried · 29 hydrogen bonds · protein-protein
- C–E · 961 Ų buried · 9 hydrogen bonds · protein-protein
- B–D · 895 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 5ENS · PDBe 5ENS · UniProt P31224
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