› 4lhe

X-ray diffraction
1.96Å resolution

Crystal structure of closed form of Monoacylglycerol Lipase

Released:
DOI: 10.2210/pdb4lhe/pdb
PDB entry 4lhe coloured by chain, front view.
PDB entry 4lhe coloured by chain, side view.
PDB entry 4lhe coloured by chain, top view.
Source organism: Bacillus sp. H-257
Primary publication:
Substrate selectivity of bacterial monoacylglycerol lipase based on crystal structure.
Tsurumura T, Tsuge H
J Struct Funct Genomics 15 83-9 (2014)
PMID: 24894647

Function and Biology Details

Reaction catalysed: 
Hydrolyzes glycerol monoesters of long-chain fatty acids
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160635 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermostable monoacylglycerol lipase Chains: A, B
Molecule details ›
Chains: A, B
Length: 250 amino acids
Theoretical weight: 27.39 KDa
Source organism: Bacillus sp. H-257
Expression system: Bacillus sp. H-257
UniProt:
  • Canonical: P82597 (Residues: 1-250; Coverage: 100%)
Sequence domains: Serine aminopeptidase, S33
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand CL 2 x CL
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21212
Unit cell:
a: 99.755Å b: 106.191Å c: 43.053Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.243 0.28
Expression system: Bacillus sp. H-257

Quick links

Citations

1 citations in other articles

Effects of Distal Mutations on the Structure, Dynamics and Catalysis of Human Monoacylglycerol Lipase.
Tyukhtenko et al. (2018)