› 1din

X-ray diffraction
1.8Å resolution

DIENELACTONE HYDROLASE AT 2.8 ANGSTROMS

Released:
DOI: 10.2210/pdb1din/pdb
PDB entry 1din coloured by chain, front view.
PDB entry 1din coloured by chain, side view.
PDB entry 1din coloured by chain, top view.
Source organism: Pseudomonas knackmussii
Primary publication:
Refined structure of dienelactone hydrolase at 1.8 A.
Pathak D, Ollis D
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
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140972 (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: alpha/beta hydrolase

Ligands and Environments

No bound ligands
1 modified residue:
Ligand CSD 1 x CSD

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.

Quick links

Citations

14 review citations

Molecular and cellular biology of cholinesterases.
Massoulié et al. (1993)
13 more

16 mentions without citation

3(10) helices in channels and other membrane proteins.
Vieira-Pires et al. (2010)
15 more