› 1cc4

X-ray diffraction
2Å resolution

PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY.

Released:
DOI: 10.2210/pdb1cc4/pdb
PDB entry 1cc4 coloured by chain, front view.
PDB entry 1cc4 coloured by chain, side view.
PDB entry 1cc4 coloured by chain, top view.
Source organism: Pseudomonas fluorescens
Primary publication:
Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability.
Eppink MH, Bunthol C, Schreuder HA, van Berkel WJ
FEBS Lett 443 251-5 (1999)
PMID: 10025942

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: 44.29 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: 71.7Å b: 146.3Å c: 88.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 not available
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

2 mentions without citation

Structure and ligand binding properties of the epoxidase component of styrene monooxygenase .
Ukaegbu et al. (2010)
1 more