Research workbench
The crystal structure of azoreductase from yersinia pestis CO92 in complex with FMN.
Analyse The crystal structure of azoreductase from yersinia pestis CO92 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- 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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