MolNFT v1 · #90744 · protein
The crystal structure of azoreductase from yersinia pestis CO92 in complex with FMN.
4ESE · FMN-dependent NADH-azoreductase: “The crystal structure of azoreductase from yersinia pestis CO92 in complex with FMN.”. X-ray diffraction, 1 ligand (FMN). MolNFT v1 #90744 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 4ESE
- Type
- protein
- Length
- 193 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FMN-dependent NADH-azoreductase
- EC
- 1.7.-.-
- UniProt
- Q8ZE60
- Ligands
- FMN
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FMN-dependent NADH-azoreductase (EC 1.7.-.-) | protein | 193 | 41% helix, 21% strand | Q8ZE60 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 3 copies · chains A
- 12P · Dodecaethylene glycol · additive · chains A
- GOL · Glycerol · additive · chains A
- IMD · Imidazole · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 4ESE · The crystal structure of azoreductase from Yersinia pestis CO92 in complex with FMN. · the same entry in another collection · chain A against A, TM-score 1.00
- Q8ZE60 · AlphaFold monomer V2.0 prediction for FMN-dependent NADH:QUINONE oxidoreductase (Q8ZE60) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q8ZE60
- Elsewhere: RCSB PDB 4ESE · PDBe 4ESE · UniProt Q8ZE60
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