› 1pxc

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZOATE HYDROXYLASE: THE TYR201PHE, TYR385PHE, AND ASN300ASP VARIANTS

Released:
DOI: 10.2210/pdb1pxc/pdb
PDB entry 1pxc coloured by chain, front view.
PDB entry 1pxc coloured by chain, side view.
PDB entry 1pxc coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, Tyr385Phe, and Asn300Asp variants.
Lah MS, Palfey BA, Schreuder HA, Ludwig ML
Biochemistry 33 1555-64 (1994)
PMID: 8312276

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-149007 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
p-hydroxybenzoate hydroxylase Chain: A
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 44.37 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Not provided
UniProt:
  • Canonical: P20586 (Residues: 1-394; Coverage: 100%)
Gene names: PA0247, 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: 71.78Å b: 146.53Å c: 88.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.178 not available
Expression system: Not provided

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Citations

3 review citations

Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase.
Entsch et al. (2005)
2 more