› 1bkw

X-ray diffraction
2.2Å resolution

p-Hydroxybenzoate hydroxylase (phbh) mutant with cys116 replaced by ser (c116s) and arg44 replaced by lys (r44k), in complex with fad and 4-hydroxybenzoic acid

Released:
DOI: 10.2210/pdb1bkw/pdb
PDB entry 1bkw coloured by chain, front view.
PDB entry 1bkw coloured by chain, side view.
PDB entry 1bkw coloured by chain, top view.
Source organism: Pseudomonas fluorescens
Primary publication:
Structure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding.
Eppink MH, Schreuder HA, Van Berkel WJ
Eur J Biochem 231 157-65 (1995)
PMID: 7628466

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-132484 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
p-hydroxybenzoate hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 44.34 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli
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
X-ray source: SIEMENS
Spacegroup: C2221
Unit cell:
a: 72.7Å b: 146.4Å c: 88.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.182 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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