› 5hym

X-ray diffraction
2.3Å resolution

3-Hydroxybenzoate 6-hydroxylase from Rhodococcus jostii in complex with phosphatidylinositol

Released:
DOI: 10.2210/pdb5hym/pdb
PDB entry 5hym coloured by chain, front view.
PDB entry 5hym coloured by chain, side view.
PDB entry 5hym coloured by chain, top view.
Source organism: Rhodococcus jostii RHA1
Primary publication:
3-Hydroxybenzoate 6-Hydroxylase from Rhodococcus jostii RHA1 Contains a Phosphatidylinositol Cofactor.
Montersino S, Te Poele E, Orru R, Westphal AH, Barendregt A, Heck AJR, van der Geize R, Dijkhuizen L, Mattevi A, van Berkel WJH
Front Microbiol 8 1110 (2017)
PMID: 28670303

Function and Biology Details

Reaction catalysed: 
Salicylate + NADH + O(2) = catechol + NAD(+) + H(2)O + CO(2)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171146 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FAD-binding domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 424 amino acids
Theoretical weight: 46.95 KDa
Source organism: Rhodococcus jostii RHA1
Expression system: Rhodococcus jostii RHA1
UniProt:
  • Canonical: Q0SFK6 (Residues: 1-399; Coverage: 100%)
Gene name: RHA1_ro01869
Sequence domains: FAD binding domain
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
2 bound ligands:
Ligand T7X 1 x T7X
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: I4122
Unit cell:
a: 106.98Å b: 106.98Å c: 143.39Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.206 0.262
Expression system: Rhodococcus jostii RHA1

Quick links

Citations

2 review citations

Harnessing Marine Biocatalytic Reservoirs for Green Chemistry Applications through Metagenomic Technologies.
Castilla et al. (2018)
1 more

2 mentions without citation

Monooxygenation of aromatic compounds by flavin-dependent monooxygenases.
Chenprakhon et al. (2019)
1 more