2jbt

X-ray diffraction
2.8Å resolution

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

Released:
Source organism: Acinetobacter baumannii
Entry authors: Alfieri A, Mattevi A

Function and Biology Details

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • 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
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: I222
Unit cell:
a: 91.987Å b: 181.263Å c: 286.208Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.235
Expression system: Escherichia coli BL21