6k5e

X-ray diffraction
2.26Å resolution

Crystal structure of BioH from Klebsiella pneumonia

Released:
Source organism: Klebsiella pneumoniae
Primary publication:
Structural insight into the carboxylesterase BioH from Klebsiella pneumoniae.
Biochem Biophys Res Commun 520 538-543 (2019)
PMID: 31615653

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-108090 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pimeloyl-[acyl-carrier protein] methyl ester esterase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 257 amino acids
Theoretical weight: 28.29 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: A6TF35 (Residues: 1-257; Coverage: 100%)
Gene names: KPN78578_37450, KPN_03782, bioH
Sequence domains: alpha/beta hydrolase fold

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: C2221
Unit cell:
a: 107.642Å b: 109.531Å c: 292.857Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.191 0.276
Expression system: Escherichia coli K-12