MolNFT v2 · #107434 · protein
Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux pump AcrB
4U95: “Coupling of remote alternating-access transport mechanisms for protons and substrates in the multidrug efflux…”. X-ray diffraction at 2. MolNFT v2 #107434 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4U95
- Type
- protein
- Length
- 3,418 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Escherichia coli; synthetic construct
- UniProt
- P31224
Structure
x-ray diffraction · resolution 2 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 1044 | — | P31224 |
| B, C | — | protein | 1033 | — | P31224 |
| D | — | protein | 156 | — | — |
| E | — | protein | 152 | — | — |
Compared structures
- 4U95 · Coupling of remote alternating-access transport mechanisms for protons and substrates in… · the same entry in another collection · chain E against E, 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 4U95 · PDBe 4U95 · UniProt P31224
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