› 1zix

X-ray diffraction
1.8Å resolution

Crystal Structure Analysis of the dienelactone hydrolase mutant (E36D, R105H, C123S, G211D, K234N)- 1.8 A

Released:
DOI: 10.2210/pdb1zix/pdb
PDB entry 1zix coloured by chain, front view.
PDB entry 1zix coloured by chain, side view.
PDB entry 1zix 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: 25.51 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

1 bound ligand:
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 48.459Å b: 70.823Å c: 77.414Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.174 0.194
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

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