› 5eow

X-ray diffraction
2.1Å resolution

Crystal Structure of 6-Hydroxynicotinic Acid 3-Monooxygenase from Pseudomonas putida KT2440

Released:
DOI: 10.2210/pdb5eow/pdb
PDB entry 5eow coloured by chain, front view.
PDB entry 5eow coloured by chain, side view.
PDB entry 5eow coloured by chain, top view.
Source organism: Pseudomonas putida KT2440
Primary publication:
Structural and Biochemical Characterization of 6-Hydroxynicotinic Acid 3-Monooxygenase, A Novel Decarboxylative Hydroxylase Involved in Aerobic Nicotinate Degradation.
Hicks KA, Yuen ME, Zhen WF, Gerwig TJ, Story RW, Kopp MC, Snider MJ
Biochemistry 55 3432-46 (2016)
PMID: 27218267

Function and Biology Details

Reaction catalysed: 
6-hydroxynicotinate + NADH + O(2) = 2,5-dihydroxypyridine + NAD(+) + H(2)O + CO(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183462 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-hydroxynicotinate 3-monooxygenase Chain: A
Molecule details ›
Chain: A
Length: 405 amino acids
Theoretical weight: 45.99 KDa
Source organism: Pseudomonas putida KT2440
Expression system: Escherichia coli
UniProt:
  • Canonical: Q88FY2 (Residues: 1-382; Coverage: 100%)
Gene names: PP_3944, nicC
Sequence domains: FAD binding domain
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
No bound ligands
1 modified residue:
Ligand MSE 12 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 47.694Å b: 69.469Å c: 115.429Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.206 0.253
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

A Novel Degradation Mechanism for Pyridine Derivatives in Alcaligenes faecalis JQ135.
Qiu et al. (2018)
5 more

3 mentions without citation

Enzyme evolution in fungal indole alkaloid biosynthesis.
Fraley et al. (2020)
2 more