3v1k

X-ray diffraction
2.13Å resolution

Crystal Structure of the H265Q mutant of a C-C hydrolase, BphD from Burkholderia xenovorans LB400.

Released:
Entry authors: Ghosh S, Bolin JT

Function and Biology Details

Reaction catalysed:
2,6-dioxo-6-phenylhexa-3-enoate + H(2)O = benzoate + 2-oxopent-4-enoate
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 286 amino acids
Theoretical weight: 32.06 KDa
Source organism: Paraburkholderia xenovorans LB400
Expression system: Escherichia coli
UniProt:
  • Canonical: P47229 (Residues: 1-286; Coverage: 100%)
Gene names: Bxe_C1186, Bxeno_C1120, bphD
Sequence domains: Alpha/beta hydrolase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P64
Unit cell:
a: 135.992Å b: 135.992Å c: 65.767Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.2 0.245
Expression system: Escherichia coli