› 2og1

X-ray diffraction
1.6Å resolution

Crystal Structure of BphD, a C-C hydrolase from Burkholderia xenovorans LB400

Released:
DOI: 10.2210/pdb2og1/pdb
PDB entry 2og1 coloured by chain, front view.
PDB entry 2og1 coloured by chain, side view.
PDB entry 2og1 coloured by chain, top view.
Source organism: Paraburkholderia xenovorans LB400
Primary publication:
Kinetic and structural insight into the mechanism of BphD, a C-C bond hydrolase from the biphenyl degradation pathway.
Horsman GP, Ke J, Dai S, Seah SY, Bolin JT, Eltis LD
Biochemistry 45 11071-86 (2006)
PMID: 16964968

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155619 (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: 32.07 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 fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand SO4 4 x SO4
Ligand GOL 1 x GOL
Ligand EOH 3 x EOH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-D
Spacegroup: P64
Unit cell:
a: 135Å b: 135Å c: 66.725Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.208 0.224
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Biodegradation of aromatic compounds: an overview of meta-fission product hydrolases.
Khajamohiddin et al. (2008)
1 more

4 mentions without citation

Characterization of a C-C bond hydrolase from Sphingomonas wittichii RW1 with novel specificities towards polychlorinated biphenyl metabolites.
Seah et al. (2007)
3 more