PDBe 1din

X-ray diffraction
1.8Å resolution

DIENELACTONE HYDROLASE AT 2.8 ANGSTROMS

Released:
Source organism: Pseudomonas knackmussii
Primary publication:
Refined structure of dienelactone hydrolase at 1.8 A.
J. Mol. Biol. 214 497-525 (1990)
PMID: 2380986

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxymethylenebutenolidase Chain: A
Molecule details ›
Chain: A
Length: 236 amino acids
Theoretical weight: 25.54 KDa
Source organism: Pseudomonas knackmussii
Expression system: Pseudomonas sp.
UniProt:
  • Canonical: P0A115 (Residues: 1-236; Coverage: 100%)
Gene name: clcD
Sequence domains: Dienelactone hydrolase family
Structure domains: Rossmann fold

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 48.9Å b: 71.45Å c: 78.24Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.15 not available
Expression system: Pseudomonas sp.