X-ray diffraction
2.8Å resolution

Structure of the monooxygenase component of p-hydroxyphenylacetate hydroxylase from Acinetobacter baumannii

Source organism: Acinetobacter baumannii

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
p-hydroxyphenylacetate 3-hydroxylase, oxygenase component Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 422 amino acids
Theoretical weight: 47 KDa
Source organism: Acinetobacter baumannii
Expression system: Escherichia coli BL21
  • Canonical: Q6Q272 (Residues: 1-422; Coverage: 100%)
Gene name: C2-hpah
Sequence domains: Acyl-CoA dehydrogenase, C-terminal domain
Structure domains:

Ligands and Environments

Cofactor: Ligand FMN 4 x FMN
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: I222
Unit cell:
a: 94.316Å b: 183.425Å c: 284.368Å
α: 90° β: 90° γ: 90°
R R work R free
0.251 0.251 0.287
Expression system: Escherichia coli BL21