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› 1zi8

X-ray diffraction
1.4Å resolution

Crystal Structure Analysis of the dienelactone hydrolase mutant(E36D, C123S, A134S, S208G, A229V, K234R)- 1.4 A

Released:
DOI: 10.2210/pdb1zi8/pdb
Model geometry
Fit model/data
PDB entry 1zi8 coloured by chain, front view.
PDB entry 1zi8 coloured by chain, side view.
PDB entry 1zi8 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: 
2-(5-oxo-2,5-dihydrofuran-2-ylidene)acetate + H2O = 4-oxohex-2-enedioate+ H(+).
Biochemical function:
Biological process:
  • not assigned
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: 25.52 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 5 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 14-BM-D
Spacegroup: P212121
Unit cell:
a: 48.494Å b: 70.408Å c: 77.219Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 0.189
Expression system: Escherichia coli

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Citations

6 citation in other articles

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

1 mention without citation

Indole Biodegradation in Acinetobacter sp. Strain O153: Genetic and Biochemical Characterization.
Sadauskas et al. (2017)