› 1t3q

X-ray diffraction
1.8Å resolution

Crystal structure of quinoline 2-Oxidoreductase from Pseudomonas Putida 86

Released:
DOI: 10.2210/pdb1t3q/pdb
PDB entry 1t3q coloured by chain, front view.
PDB entry 1t3q coloured by chain, side view.
PDB entry 1t3q coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Active site geometry and substrate recognition of the molybdenum hydroxylase quinoline 2-oxidoreductase.
Bonin I, Martins BM, Purvanov V, Fetzner S, Huber R, Dobbek H
Structure 12 1425-35 (2004)
PMID: 15296736

Function and Biology Details

Reaction catalysed: 
Quinoline + acceptor + H(2)O = quinolin-2(1H)-one + reduced acceptor
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-159837 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
2Fe-2S ferredoxin-type domain-containing protein Chains: A, D
Molecule details ›
Chains: A, D
Length: 168 amino acids
Theoretical weight: 18.04 KDa
Source organism: Pseudomonas putida
UniProt:
  • Canonical: P72223 (Residues: 1-168; Coverage: 100%)
Gene name: qorS
Sequence domains:
Structure domains:
Aldehyde oxidase/xanthine dehydrogenase a/b hammerhead domain-containing protein Chains: B, E
Molecule details ›
Chains: B, E
Length: 788 amino acids
Theoretical weight: 84.26 KDa
Source organism: Pseudomonas putida
UniProt:
  • Canonical: P72224 (Residues: 1-788; Coverage: 100%)
Gene name: qorL
Sequence domains:
Structure domains:
FAD-binding PCMH-type domain-containing protein Chains: C, F
Molecule details ›
Chains: C, F
Length: 288 amino acids
Theoretical weight: 30.71 KDa
Source organism: Pseudomonas putida
UniProt:
  • Canonical: P72222 (Residues: 1-288; Coverage: 100%)
Gene names: KF715C_ch5940, qorM
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD

Cofactor: Ligand MCN 2 x MCN
4 bound ligands:
Ligand FES 4 x FES
Ligand GOL 9 x GOL
Ligand SO4 8 x SO4
Ligand SMO 2 x SMO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: C2
Unit cell:
a: 278.32Å b: 72.1Å c: 202.65Å
α: 90° β: 127.98° γ: 90°
R-values:
R R work R free
0.186 0.186 0.207

Quick links

Citations

6 review citations

Anaerobic catabolism of aromatic compounds: a genetic and genomic view.
Carmona et al. (2009)
5 more

5 mentions without citation

The mononuclear molybdenum enzymes.
Hille et al. (2014)
4 more