› 1zj5

X-ray diffraction
1.7Å resolution

Crystal Structure Analysis of the dienelactone hydrolase mutant (E36D, C123S, A134S, S208G, A229V, K234R) bound with the PMS moiety of the protease inhibitor, Phenylmethylsulfonyl fluoride (PMSF)- 1.7 A

Released:
DOI: 10.2210/pdb1zj5/pdb
PDB entry 1zj5 coloured by chain, front view.
PDB entry 1zj5 coloured by chain, side view.
PDB entry 1zj5 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: 25.68 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 2 x SO4
Ligand GOL 1 x GOL
1 modified residue:
Ligand SEB 1 x SEB

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 47.549Å b: 70.658Å c: 77.627Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.184 0.21
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

1 mention without citation

Carboxylic ester hydrolases: Classification and database derived from their primary, secondary, and tertiary structures.
Chen et al. (2016)