› 1zi9

X-ray diffraction
1.5Å resolution

Crystal Structure Analysis of the dienelactone hydrolase (E36D, C123S) mutant- 1.5 A

Released:
DOI: 10.2210/pdb1zi9/pdb
PDB entry 1zi9 coloured by chain, front view.
PDB entry 1zi9 coloured by chain, side view.
PDB entry 1zi9 coloured by chain, top view.
Source organism: Pseudomonas putida
Primary publication:
Following directed evolution with crystallography: structural changes observed in changing the substrate specificity of dienelactone hydrolase.
Kim HK, Liu JW, Carr PD, Ollis DL
Acta Crystallogr D Biol Crystallogr 61 920-31 (2005)
PMID: 15983415

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
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: 25.48 KDa
Source organism: Pseudomonas putida
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A114 (Residues: 1-236; Coverage: 100%)
Gene name: clcD
Sequence domains: Dienelactone hydrolase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand SO4 1 x SO4
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-D
Spacegroup: P212121
Unit cell:
a: 48.411Å b: 70.912Å c: 76.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.173 0.198
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Ultrahigh-throughput discovery of promiscuous enzymes by picodroplet functional metagenomics.
Colin et al. (2015)
4 more

1 mention without citation

Distinctive structural motifs co-ordinate the catalytic nucleophile and the residues of the oxyanion hole in the alpha/beta-hydrolase fold enzymes.
Dimitriou et al. (2019)