› 5hxi

X-ray diffraction
1.5Å resolution

2-Methyl-3-hydroxypyridine-5-carboxylic acid oxygenase, 5HN bound

Released:
DOI: 10.2210/pdb5hxi/pdb
PDB entry 5hxi coloured by chain, front view.
PDB entry 5hxi coloured by chain, side view.
PDB entry 5hxi coloured by chain, top view.
Source organism: Mesorhizobium japonicum MAFF 303099
Primary publication:
Role of the Tyr270 residue in 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase from Mesorhizobium loti.
Kobayashi J, Yoshida H, Yagi T, Kamitori S, Hayashi H, Mizutani K, Takahashi N, Mikami B
J Biosci Bioeng 123 154-162 (2017)
PMID: 27568368

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189132 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD-binding domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 379 amino acids
Theoretical weight: 41.8 KDa
Source organism: Mesorhizobium japonicum MAFF 303099
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q988D3 (Residues: 1-379; Coverage: 100%)
Gene name: mlr6788
Sequence domains: FAD binding domain
Structure domains:

Ligands and Environments

6 bound ligands:
Ligand FAD 1 x FAD
Ligand BME 1 x BME
Ligand 5HN 1 x 5HN
Ligand NA 2 x NA
Ligand GOL 4 x GOL
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: I222
Unit cell:
a: 49.338Å b: 131.14Å c: 132.282Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.152 0.151 0.174
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Monooxygenation of aromatic compounds by flavin-dependent monooxygenases.
Chenprakhon et al. (2019)
2 other articles

1 mention without citation

Structural comparison of p-hydroxybenzoate hydroxylase (PobA) from Pseudomonas putida with PobA from other Pseudomonas spp. and other monooxygenases.
Lazar et al. (2019)