1dt5

X-ray diffraction
2.4Å resolution

THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE

Released:

Function and Biology Details

Reaction catalysed:
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 269 amino acids
Theoretical weight: 29.34 KDa
Source organism: Thermomyces lanuginosus
UniProt:
  • Canonical: O59952 (Residues: 23-291; Coverage: 98%)
Gene name: LIP
Sequence domains: Lipase (class 3)
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P21
Unit cell:
a: 85.435Å b: 162.878Å c: 86.717Å
α: 90° β: 98.45° γ: 90°
R-values:
R R work R free
0.244 0.244 0.315