› 1pdh

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE RECONSTITUTED WITH THE MODIFIED FAD PRESENT IN ALCOHOL OXIDASE FROM METHYLOTROPHIC YEASTS: EVIDENCE FOR AN ARABINOFLAVIN

Released:
DOI: 10.2210/pdb1pdh/pdb
PDB entry 1pdh coloured by chain, front view.
PDB entry 1pdh coloured by chain, side view.
PDB entry 1pdh coloured by chain, top view.
Source organism: Pseudomonas fluorescens
Primary publication:
Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin.
van Berkel WJ, Eppink MH, Schreuder HA
Protein Sci 3 2245-53 (1994)
PMID: 7756982

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-132485 (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 FAS 1 x FAS
1 bound ligand:
Ligand PHB 1 x PHB
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 72.1Å b: 146.4Å c: 88.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 not available
Expression system: Not provided

Quick links

Citations

6 review citations

Control of catalysis in flavin-dependent monooxygenases.
Palfey et al. (2010)
5 more

1 mention without citation

Pyridine Nucleotide Coenzyme Specificity of p-Hydroxybenzoate Hydroxylase and Related Flavoprotein Monooxygenases.
Westphal et al. (2018)