› 2rht

X-ray diffraction
1.7Å resolution

Crystal Structure of the S112A mutant of a C-C hydrolase, BphD from Burkholderia xenovorans LB400, in complex with 3-Cl HOPDA

Released:
DOI: 10.2210/pdb2rht/pdb
PDB entry 2rht coloured by chain, front view.
PDB entry 2rht coloured by chain, side view.
PDB entry 2rht coloured by chain, top view.
Source organism: Paraburkholderia xenovorans LB400
Primary publication:
The molecular basis for inhibition of BphD, a C-C bond hydrolase involved in polychlorinated biphenyls degradation: large 3-substituents prevent tautomerization.
Bhowmik S, Horsman GP, Bolin JT, Eltis LD
J Biol Chem 282 36377-85 (2007)
PMID: 17932031

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 domain:

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 Chain: A
Molecule details ›
Chain: A
Length: 283 amino acids
Theoretical weight: 31.75 KDa
Source organism: Paraburkholderia xenovorans LB400
UniProt:
  • Canonical: P47229 (Residues: 4-286; Coverage: 99%)
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 NA 1 x NA
Ligand C1E 1 x C1E
Ligand MLI 1 x MLI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: I4122
Unit cell:
a: 117.774Å b: 117.774Å c: 86.739Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.153 0.189

Quick links

Citations

2 review citations

The alpha/beta-hydrolase fold 3DM database (ABHDB) as a tool for protein engineering.
Kourist et al. (2010)
1 more

1 mention without citation

The lid domain of the MCP hydrolase DxnB2 contributes to the reactivity toward recalcitrant PCB metabolites.
Ruzzini et al. (2013)