4ke9

X-ray diffraction
2.2Å resolution

Crystal structure of Monoglyceride lipase from Bacillus sp. H257 in complex with an 1-stearyol glycerol analogue

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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 268 amino acids
Theoretical weight: 29.34 KDa
Source organism: Bacillus sp. H-257
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P82597 (Residues: 3-250; Coverage: 99%)
Sequence domains: Serine aminopeptidase, S33
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 76.857Å b: 80.287Å c: 85.712Å
α: 90° β: 100.02° γ: 90°
R-values:
R R work R free
0.225 0.223 0.262
Expression system: Escherichia coli BL21(DE3)