X-ray diffraction
2Å resolution

Crystal structure of a putative DAG-like lipase (MgMDL2) from Malassezia globosa

Source organism: Malassezia globosa CBS 7966
Primary publication:
Malassezia globosa MgMDL2 lipase: Crystal structure and rational modification of substrate specificity.
Biochem. Biophys. Res. Commun. 488 259-265 (2017)
PMID: 28433636

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lipase_3 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 286 amino acids
Theoretical weight: 31.83 KDa
Source organism: Malassezia globosa CBS 7966
Expression system: Komagataella pastoris
  • Canonical: A8PUY5 (Residues: 19-304; Coverage: 100%)
Gene name: MGL_0799
Sequence domains: Lipase (class 3)
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 76.97Å b: 82.32Å c: 116.87Å
α: 90° β: 90° γ: 90°
R R work R free
0.19 0.188 0.22
Expression system: Komagataella pastoris