› 1doc

X-ray diffraction
2Å resolution

THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS

Released:
DOI: 10.2210/pdb1doc/pdb
PDB entry 1doc coloured by chain, front view.
PDB entry 1doc coloured by chain, side view.
PDB entry 1doc coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
The mobile flavin of 4-OH benzoate hydroxylase.
Gatti DL, Palfey BA, Lah MS, Entsch B, Massey V, Ballou DP, Ludwig ML
Science 266 110-4 (1994)
PMID: 7939628

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: 44.38 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
2 bound ligands:
Ligand BR 3 x BR
Ligand PHB 1 x PHB
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 71.68Å b: 146.72Å c: 88.09Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.173 not available
Expression system: Not provided

Quick links

Citations

16 review citations

Binding of small-molecule ligands to proteins: "what you see" is not always "what you get".
Mobley et al. (2009)
15 more

4 mentions without citation

Mechanism and kinetics of inducible nitric oxide synthase auto-S-nitrosation and inactivation.
Smith et al. (2012)
3 more