› 2xua

X-ray diffraction
1.9Å resolution

Crystal structure of the enol-lactonase from Burkholderia xenovorans LB400

Released:
DOI: 10.2210/pdb2xua/pdb
PDB entry 2xua coloured by chain, front view.
PDB entry 2xua coloured by chain, side view.
PDB entry 2xua coloured by chain, top view.
Source organism: Paraburkholderia xenovorans LB400
Primary publication:
A product analog bound form of 3-oxoadipate-enol-lactonase (PcaD) reveals a multifunctional role for the divergent cap domain.
Bains J, Kaufman L, Farnell B, Boulanger MJ
J Mol Biol 406 649-58 (2011)
PMID: 21237173

Function and Biology Details

Reaction catalysed: 
3-oxoadipate enol-lactone + H(2)O = 3-oxoadipate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171868 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chains: A, H
Molecule details ›
Chains: A, H
Length: 266 amino acids
Theoretical weight: 29.18 KDa
Source organism: Paraburkholderia xenovorans LB400
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q13KT2 (Residues: 1-263; Coverage: 100%)
Gene names: Bxe_B0646, pcaD
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand SHF 1 x SHF
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21212
Unit cell:
a: 66.72Å b: 101.16Å c: 72.52Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.183 0.241
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

The karrikin response system of Arabidopsis.
Waters et al. (2014)
1 more

11 mentions without citation

Enzymes from Extreme Environments and Their Industrial Applications.
Littlechild JA. (2015)
10 more