› 1m33

X-ray diffraction
1.7Å resolution

Function and Biology Details

Reaction catalysed: 
Pimeloyl-[acyl-carrier protein] methyl ester + H(2)O = pimeloyl-[acyl-carrier protein] + methanol
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146427 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pimeloyl-[acyl-carrier protein] methyl ester esterase Chain: A
Molecule details ›
Chain: A
Length: 258 amino acids
Theoretical weight: 28.97 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P13001 (Residues: 1-256; Coverage: 100%)
Gene names: JW3375, b3412, bioB, bioH
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand 3OH 1 x 3OH
Ligand EDO 2 x EDO
1 modified residue:
Ligand MSE 6 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P43
Unit cell:
a: 75.21Å b: 75.21Å c: 49.256Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.145 0.188
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Searching for functional sites in protein structures.
Jones et al. (2004)
12 more

21 mentions without citation

Integrating structure, bioinformatics, and enzymology to discover function: BioH, a new carboxylesterase from Escherichia coli.
Sanishvili et al. (2003)
20 more