4p92

X-ray diffraction
1.65Å resolution

Crystal structure of dienelactone hydrolase C123S mutant at 1.65 A resolution

Released:
Source organism: Pseudomonas putida
Primary publication:
Crystallization of dienelactone hydrolase in two space groups: structural changes caused by crystal packing.
Acta Crystallogr F Struct Biol Commun 70 884-9 (2014)
PMID: 25005082

Function and Biology Details

Reaction catalysed:
4-carboxymethylenebut-2-en-4-olide + H(2)O = 4-oxohex-2-enedioate
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-140971 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxymethylenebutenolidase Chain: A
Molecule details ›
Chain: A
Length: 236 amino acids
Theoretical weight: 25.5 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli DH5[alpha]
UniProt:
  • Canonical: P0A114 (Residues: 1-236; Coverage: 100%)
Gene name: clcD
Sequence domains: Dienelactone hydrolase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: P212121
Unit cell:
a: 48.23Å b: 70.98Å c: 77.46Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.158 0.158 0.172
Expression system: Escherichia coli DH5[alpha]