1cj2

X-ray diffraction
2.8Å resolution

MUTANT GLN34ARG OF PARA-HYDROXYBENZOATE HYDROXYLASE

Released:
Source organism: Pseudomonas fluorescens
Primary publication:
Switch of coenzyme specificity of p-hydroxybenzoate hydroxylase.
J. Mol. Biol. 292 87-96 (1999)
PMID: 10493859

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
p-hydroxybenzoate hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 391 amino acids
Theoretical weight: 44.02 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00438 (Residues: 1-391; Coverage: 99%)
Gene name: pobA
Sequence domains: FAD binding domain
Structure domains:

Ligands and Environments


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

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: C2221
Unit cell:
a: 71.8Å b: 146.5Å c: 88.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.144 0.144 not available
Expression system: Escherichia coli