› 3v1l

X-ray diffraction
2.11Å resolution

Crystal Structure of the S112A/H265Q mutant of a C-C hydrolase, BphD from Burkholderia xenovorans LB400

Released:
DOI: 10.2210/pdb3v1l/pdb
PDB entry 3v1l coloured by chain, front view.
PDB entry 3v1l coloured by chain, side view.
PDB entry 3v1l coloured by chain, top view.
Source organism: Paraburkholderia xenovorans LB400
Primary publication:
Identification of an acyl-enzyme intermediate in a meta-cleavage product hydrolase reveals the versatility of the catalytic triad.
Ruzzini AC, Ghosh S, Horsman GP, Foster LJ, Bolin JT, Eltis LD
J Am Chem Soc 134 4615-24 (2012)
PMID: 22339283

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 Chain: A
Molecule details ›
Chain: A
Length: 286 amino acids
Theoretical weight: 32.04 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 MLA 1 x MLA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: I4122
Unit cell:
a: 117.458Å b: 117.458Å c: 87.791Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.179 0.219
Expression system: Escherichia coli

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Citations

1 review citation

Prospects for using combined engineered bacterial enzymes and plant systems to rhizoremediate polychlorinated biphenyls.
Sylvestre M. (2013)
15 other articles