› 1oil

X-ray diffraction
2.1Å resolution

Function and Biology Details

Reaction catalysed: 
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149521 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triacylglycerol lipase Chains: A, B
Molecule details ›
Chains: A, B
Length: 320 amino acids
Theoretical weight: 33.15 KDa
Source organism: Burkholderia cepacia
UniProt:
  • Canonical: P22088 (Residues: 45-364; Coverage: 100%)
Gene names: lip, lipA
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 85.23Å b: 47.42Å c: 86.53Å
α: 90° β: 116.11° γ: 90°
R-values:
R R work R free
0.18 0.18 0.255

Quick links

Citations

10 review citations

Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases.
Jaeger et al. (1999)
9 more

11 mentions without citation

Dieselzymes: development of a stable and methanol tolerant lipase for biodiesel production by directed evolution.
Korman et al. (2013)
10 more