› 4ou4

X-ray diffraction
2.4Å resolution

Crystal structure of esterase rPPE mutant S159A complexed with (S)-Ac-CPA

Released:
DOI: 10.2210/pdb4ou4/pdb
PDB entry 4ou4 coloured by chain, front view.
PDB entry 4ou4 coloured by chain, side view.
PDB entry 4ou4 coloured by chain, top view.
Source organism: Pseudomonas sp. ECU1011
Primary publication:
Crystal structures of Pseudomonas putida esterase reveal the functional role of residues 187 and 287 in substrate binding and chiral recognition.
Dou S, Kong XD, Ma BD, Chen Q, Zhang J, Zhou J, Xu JH
Biochem Biophys Res Commun 446 1145-50 (2014)
PMID: 24680822

Function and Biology Details

Reaction catalysed: 
A carboxylic ester + H(2)O = an alcohol + a carboxylate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125836 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha/beta hydrolase fold-3 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 338 amino acids
Theoretical weight: 36.53 KDa
Source organism: Pseudomonas sp. ECU1011
Expression system: Escherichia coli
UniProt:
  • Canonical: L7PYQ2 (Residues: 1-316; Coverage: 100%)
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand S2T 1 x S2T
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P43212
Unit cell:
a: 94.624Å b: 94.624Å c: 88.533Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.167 0.234
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Esterases as stereoselective biocatalysts.
Romano et al. (2015)
13 other articles

1 mention without citation

The first description of a hormone-sensitive lipase from a basidiomycete: Structural insights and biochemical characterization revealed Bjerkandera adusta BaEstB as a novel esterase.
Sánchez-Carbente et al. (2017)