› 1pbe

X-ray diffraction
1.9Å resolution

CRYSTAL STRUCTURE OF THE P-HYDROXYBENZOATE HYDROXYLASE-SUBSTRATE COMPLEX REFINED AT 1.9 ANGSTROMS RESOLUTION. ANALYSIS OF THE ENZYME-SUBSTRATE AND ENZYME-PRODUCT COMPLEXES

Released:
DOI: 10.2210/pdb1pbe/pdb
PDB entry 1pbe coloured by chain, front view.
PDB entry 1pbe coloured by chain, side view.
PDB entry 1pbe coloured by chain, top view.
Source organism: Pseudomonas fluorescens
Primary publication:
Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. Analysis of the enzyme-substrate and enzyme-product complexes.
Schreuder HA, Prick PA, Wierenga RK, Vriend G, Wilson KS, Hol WG, Drenth J
J Mol Biol 208 679-96 (1989)
PMID: 2553983

Function and Biology Details

Reaction catalysed: 
4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-523480 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
p-hydroxybenzoate hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 44.38 KDa
Source organism: Pseudomonas fluorescens
Expression system: Not provided
UniProt:
  • Canonical: P00438 (Residues: 1-394; Coverage: 100%)
Gene name: pobA
Sequence domains: FAD binding domain
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
Ligand PHB 1 x PHB
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 71.5Å b: 145.8Å c: 88.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 not available not available
Expression system: Not provided

Quick links

Citations

9 review citations

Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts.
van Berkel et al. (2006)
8 more

37 mentions without citation

Form follows function: structural and catalytic variation in the class a flavoprotein monooxygenases.
Crozier-Reabe et al. (2012)
36 more