Research workbench
X-ray crystallographic structure of a pseudomonas aeruginosa azoreductase in complex with methyl red.
Analyse X-ray crystallographic structure of a pseudomonas aeruginosa azoreductase in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V9C
- Type
- protein
- Length
- 396 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FMN-dependent NADH-azoreductase 1
- EC
- 1.7.1.6
- UniProt
- Q9I5F3
- Ligands
- FMN, MRE
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FMN-dependent NADH-azoreductase 1 (EC 1.7.1.6) | protein | 203 | 40% helix, 22% strand | Q9I5F3 |
| B | FMN-dependent NADH-azoreductase 1 (EC 1.7.1.6) | protein | 193 | 40% helix, 22% strand | Q9I5F3 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- MRE · 2-(4-dimethylaminophenyl)diazenylbenzoic acid · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 429 | 0.70 | 0.81 | 38 | FMN, MRE |
| 2 | 435 | 0.69 | 0.80 | 32 | FMN, MRE |
| 3 | 125 | 0.51 | 0.81 | 38 | GOL |
Interfaces
1 interface between chains.
- A–B · 1295 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2V9C · X-ray Crystallographic Structure of a Pseudomonas aeruginosa Azoreductase in Complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9I5F3 · AlphaFold monomer V2.0 prediction for FMN-dependent NAD(P)H:QUINONE oxidoreductase 1… · a predicted model of the same protein · chain B 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 Q9I5F3
- Elsewhere: RCSB PDB 2V9C · PDBe 2V9C · UniProt Q9I5F3
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