MolNFT v1 · #159120 · protein
Structural basis for multidrug recognition and antimicrobial resistance by mtrr, an efflux pump regulator from neisseria gonorrhoeae
6OF0: “Structural basis for multidrug recognition and antimicrobial resistance by mtrr, an efflux pump regulator…”. X-ray diffraction, 1 ligand (PO4). MolNFT v1 #159120 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6OF0
- Type
- protein
- Length
- 783 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P39897
- Ligands
- PO4
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 192 | — | P39897 |
| B | — | protein | 196 | — | P39897 |
| C | — | protein | 201 | — | P39897 |
| D | — | protein | 194 | — | P39897 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · 6 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6OF0 · Structural basis for multidrug recognition and antimicrobial resistance by MTRR, an… · the same entry in another collection · chain D against D, TM-score 1.00
- P39897 · AlphaFold monomer V2.0 prediction for hth-type transcriptional regulator mtrr (P39897) · a predicted model of the same protein · chain D 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 P39897
- Elsewhere: RCSB PDB 6OF0 · PDBe 6OF0 · UniProt P39897
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