1f6w

X-ray diffraction
2.3Å resolution

STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN BILE SALT ACTIVATED LIPASE

Released:
Source organism: Homo sapiens

Function and Biology Details

Reactions catalysed:
A steryl ester + H(2)O = a sterol + a fatty acid
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
An acetic ester + H(2)O = an alcohol + acetate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-148760 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bile salt-activated lipase Chain: A
Molecule details ›
Chain: A
Length: 533 amino acids
Theoretical weight: 58.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P19835 (Residues: 21-553; Coverage: 73%)
Gene names: BAL, CEL
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P212121
Unit cell:
a: 64.7Å b: 88.97Å c: 104.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.267
Expression system: Escherichia coli