› 3cn7

X-ray diffraction
2.99Å resolution

Crystal Structure Analysis of the Carboxylesterase PA3859 from Pseudomonas aeruginosa PAO1- MONOCLINIC CRYSTAL FORM

Released:
DOI: 10.2210/pdb3cn7/pdb
PDB entry 3cn7 coloured by chain, front view.
PDB entry 3cn7 coloured by chain, side view.
PDB entry 3cn7 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Insights into the fatty acid chain length specificity of the carboxylesterase PA3859 from Pseudomonas aeruginosa: A combined structural, biochemical and computational study.
Pesaresi A, Lamba D
Biochimie 92 1787-92 (2010)
PMID: 20850500

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191103 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phospholipase/carboxylesterase/thioesterase domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 226 amino acids
Theoretical weight: 24.72 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9HXE7 (Residues: 2-215; Coverage: 100%)
Gene name: PA3859
Sequence domains: Phospholipase/Carboxylesterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand MES 2 x MES
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: P21
Unit cell:
a: 65.649Å b: 50.548Å c: 142.548Å
α: 90° β: 92.94° γ: 90°
R-values:
R R work R free
0.204 0.204 0.274
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Evolution of a new function in an esterase: simple amino acid substitutions enable the activity present in the larger paralog, BioH.
Flores et al. (2012)
3 more

7 mentions without citation

Thioesterases: a new perspective based on their primary and tertiary structures.
Cantu et al. (2010)
6 more