› 2pu5

X-ray diffraction
2.3Å resolution

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

Released:
DOI: 10.2210/pdb2pu5/pdb
PDB entry 2pu5 coloured by chain, front view.
PDB entry 2pu5 coloured by chain, side view.
PDB entry 2pu5 coloured by chain, top view.
Source organism: Paraburkholderia xenovorans LB400
Primary publication:
The tautomeric half-reaction of BphD, a C-C bond hydrolase. Kinetic and structural evidence supporting a key role for histidine 265 of the catalytic triad.
Horsman GP, Bhowmik S, Seah SY, Kumar P, Bolin JT, Eltis LD
J Biol Chem 282 19894-904 (2007)
PMID: 17442675

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

1 bound ligand:
Ligand MLI 2 x MLI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P64
Unit cell:
a: 135.183Å b: 135.183Å c: 66.268Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.176 0.27
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Biosynthesis, synthesis, and biological activities of pyrrolobenzodiazepines.
Gerratana B. (2012)
2 more

1 mention without citation

Excellent Degradation Performance of a Versatile Phthalic Acid Esters-Degrading Bacterium and Catalytic Mechanism of Monoalkyl Phthalate Hydrolase.
Fan et al. (2018)