› 6ax1

X-ray diffraction
2.26Å resolution

Structure of human monoacylglycerol lipase bound to a covalent inhibitor

Released:
DOI: 10.2210/pdb6ax1/pdb
PDB entry 6ax1 coloured by chain, front view.
PDB entry 6ax1 coloured by chain, side view.
PDB entry 6ax1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Azetidine and Piperidine Carbamates as Efficient, Covalent Inhibitors of Monoacylglycerol Lipase.
Butler CR, Beck EM, Harris A, Huang Z, McAllister LA, Am Ende CW, Fennell K, Foley TL, Fonseca K, Hawrylik SJ, Johnson DS, Knafels JD, Mente S, Noell GS, Pandit J, Phillips TB, Piro JR, Rogers BN, Samad TA, Wang J, Wan S, Brodney MA
J Med Chem 60 9860-9873 (2017)
PMID: 29148769

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: 348 amino acids
Theoretical weight: 38.26 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
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand C0S 2 x C0S
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: I222
Unit cell:
a: 86.36Å b: 126.9Å c: 137.51Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.163 0.198
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Monoacylglycerol lipase inhibitors: modulators for lipid metabolism in cancer malignancy, neurological and metabolic disorders.
Deng et al. (2020)
1 more

3 mentions without citation

Characterization of a monoacylglycerol lipase in the medicinal leech, Hirudo verbana.
Kabeiseman et al. (2020)
2 more