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The crystal structure of an FMN-dependent NADH:QUINONE oxidoreductase, azor from escherichia COLI
Analyse The crystal structure of an FMN-dependent NADH:QUINONE oxidoreductase, azor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N2X
- Type
- protein
- Length
- 201 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FMN-dependent NADH:QUINONE oxidoreductase
- EC
- 1.6.5.-, 1.7.1.17
- UniProt
- Q8X9S9
- Ligands
- FMN, DHA, P4G
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FMN-dependent NADH:QUINONE oxidoreductase (EC 1.6.5.-, 1.7.1.17) | protein | 201 | 43% helix, 20% strand | Q8X9S9 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- DHA · 2-amino-acrylic acid · ligand · chains A
- P4G · 1-ethoxy-2-(2-ethoxyethoxy)ethane · ligand · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7N2X · The crystal structure of an FMN-dependent NADH:qui oxidoreductase, AzoR from Escherichia… · the same entry in another collection · chain A against A, TM-score 1.00
- Q8X9S9 · AlphaFold monomer V2.0 prediction for FMN-dependent NADH:QUINONE oxidoreductase (Q8X9S9) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 Q8X9S9
- Elsewhere: RCSB PDB 7N2X · PDBe 7N2X · UniProt Q8X9S9
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