5e4y

X-ray diffraction
2.8Å resolution

Orthorhombic structure of the acetyl esterase MekB

Released:

Function and Biology Details

Reaction catalysed:
Ethyl acetate + H(2)O = acetate + ethanol
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-170988 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ethyl acetate hydrolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 361 amino acids
Theoretical weight: 39.75 KDa
Source organism: Pseudomonas veronii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q0MRG5 (Residues: 2-349; Coverage: 100%)
Gene name: mekB
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 58.346Å b: 79.946Å c: 142.177Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.237
Expression system: Escherichia coli