› 4uuq

X-ray diffraction
2.36Å resolution

Function and Biology Details

Reaction catalysed: 
Hydrolyzes glycerol monoesters of long-chain fatty acids
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189246 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Monoglyceride lipase Chains: A, B
Molecule details ›
Chains: A, B
Length: 320 amino acids
Theoretical weight: 35.29 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99685 (Residues: 1-303; Coverage: 100%)
Gene name: MGLL
Sequence domains: Serine aminopeptidase, S33
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand 64D 2 x 64D
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: I222
Unit cell:
a: 86.25Å b: 126.26Å c: 138.62Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.21 0.259
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

24 review citations

Cannabinoids and the expanded endocannabinoid system in neurological disorders.
Cristino et al. (2020)
23 more

5 mentions without citation

Carboxylic ester hydrolases: Classification and database derived from their primary, secondary, and tertiary structures.
Chen et al. (2016)
4 more