› 3ia2

X-ray diffraction
1.65Å resolution

Pseudomonas fluorescens esterase complexed to the R-enantiomer of a sulfonate transition state analog

Released:
DOI: 10.2210/pdb3ia2/pdb
PDB entry 3ia2 coloured by chain, front view.
PDB entry 3ia2 coloured by chain, side view.
PDB entry 3ia2 coloured by chain, top view.
Source organism: Pseudomonas fluorescens
Primary publication:
Different active-site loop orientation in serine hydrolases versus acyltransferases.
Jiang Y, Morley KL, Schrag JD, Kazlauskas RJ
Chembiochem 12 768-76 (2011)
PMID: 21351219

Function and Biology Details

Reaction catalysed: 
A phenyl acetate + H(2)O = a phenol + acetate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149815 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arylesterase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 271 amino acids
Theoretical weight: 29.99 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli
UniProt:
  • Canonical: P22862 (Residues: 2-272; Coverage: 100%)
Gene name: estF
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand J6Z 6 x J6Z
Ligand GOL 25 x GOL
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P32
Unit cell:
a: 146.215Å b: 146.215Å c: 129.964Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.197 0.208
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Polyketide synthase and non-ribosomal peptide synthetase thioesterase selectivity: logic gate or a victim of fate?
Horsman et al. (2016)
2 more

5 mentions without citation

How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes.
Rauwerdink et al. (2015)
4 more