› 1gpl

X-ray diffraction
2.01Å resolution

Function and Biology Details

Reactions catalysed: 
1,2-diacyl-3-beta-D-galactosyl-sn-glycerol + 2 H(2)O = 3-beta-D-galactosyl-sn-glycerol + 2 carboxylates
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147662 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pancreatic lipase-related protein 2; Pancreatic triacylglycerol lipase Chain: A
Molecule details ›
Chain: A
Length: 432 amino acids
Theoretical weight: 47.88 KDa
Source organisms: Expression system: SF9 CELLS
UniProt:
  • Canonical: P81139 (Residues: 1-326; Coverage: 75%)
  • Canonical: P16233 (Residues: 360-465; Coverage: 24%)
Gene names: PNLIP, PNLIPRP2
Sequence domains:
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 62Å b: 55.9Å c: 144Å
α: 90° β: 93.2° γ: 90°
R-values:
R R work R free
0.188 0.188 0.246
Expression system: SF9 CELLS

Quick links

Citations

8 review citations

Lipase protein engineering.
Svendsen A. (2000)
7 more

10 mentions without citation

The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties.
Khan et al. (2017)
9 more