› 6qpp

X-ray diffraction
1.49Å resolution

Function and Biology Details

Reaction catalysed: 
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148621 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipase Chain: A
Molecule details ›
Chain: A
Length: 363 amino acids
Theoretical weight: 39.63 KDa
Source organism: Rhizomucor miehei
Expression system: Aspergillus oryzae
UniProt:
  • Canonical: P19515 (Residues: 1-363; Coverage: 100%)
Sequence domains: Lipase (class 3)

Ligands and Environments

2 bound ligands:
Ligand NAG 1 x NAG
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: C2
Unit cell:
a: 98.04Å b: 61.02Å c: 62.65Å
α: 90° β: 111.97° γ: 90°
R-values:
R R work R free
0.14 0.138 0.178
Expression system: Aspergillus oryzae

Quick links

Citations

1 review citation

Cold Active Lipases: Biocatalytic Tools for Greener Technology.
Mhetras et al. (2021)
3 other articles

2 mentions without citation

Novel Inhibitory Function of the Rhizomucor miehei Lipase Propeptide and Three-Dimensional Structures of Its Complexes with the Enzyme.
Moroz et al. (2019)
1 more