› 4ob6

X-ray diffraction
1.7Å resolution

Complex structure of esterase rPPE S159A/W187H and substrate (S)-Ac-CPA

Released:
DOI: 10.2210/pdb4ob6/pdb
PDB entry 4ob6 coloured by chain, front view.
PDB entry 4ob6 coloured by chain, side view.
PDB entry 4ob6 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

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: 341 amino acids
Theoretical weight: 36.81 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 3 x S2T
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P43212
Unit cell:
a: 95.438Å b: 95.438Å c: 88.297Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.164 0.181
Expression system: Escherichia coli

Quick links

Citations

1 review citation

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

2 mentions without citation

Structure and evolutionary trace-assisted screening of a residue swapping the substrate ambiguity and chiral specificity in an esterase.
Cea-Rama et al. (2021)
1 more