3rli

X-ray diffraction
1.85Å resolution

Crystal structure of monoacylglycerol lipase from Bacillus sp. H257 in complex with PMSF

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-160635 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thermostable monoacylglycerol lipase Chain: A
Molecule details ›
Chain: A
Length: 270 amino acids
Theoretical weight: 29.56 KDa
Source organism: Bacillus sp. H-257
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P82597 (Residues: 1-250; Coverage: 100%)
Sequence domains: Serine aminopeptidase, S33
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X13
Spacegroup: P21
Unit cell:
a: 38.05Å b: 70.69Å c: 43.44Å
α: 90° β: 111.65° γ: 90°
R-values:
R R work R free
0.158 0.156 0.194
Expression system: Escherichia coli BL21(DE3)