› 7l4t

X-ray diffraction
2.2Å 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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189244 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Monoglyceride lipase Chains: A, B
Molecule details ›
Chains: A, B
Length: 320 amino acids
Theoretical weight: 35.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99685 (Residues: 1-303; Coverage: 100%)
Gene name: MGLL
Sequence domains: Serine aminopeptidase, S33

Ligands and Environments

3 bound ligands:
Ligand XPD 1 x XPD
Ligand ACT 2 x ACT
Ligand MPD 4 x MPD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: I222
Unit cell:
a: 91.818Å b: 127.378Å c: 136.084Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.176 0.226
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Endocannabinoid signaling in the central nervous system.
Martinez Ramirez et al. (2023)
5 more

1 mention without citation

Discovery of 8-prenylnaringenin from hop (Humulus lupulus L.) as a potent monoacylglycerol lipase inhibitor for treatments of neuroinflammation and Alzheimer's disease.
Tung et al. (2021)