› 1dte

X-ray diffraction
2.35Å resolution

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

Released:
DOI: 10.2210/pdb1dte/pdb
PDB entry 1dte coloured by chain, front view.
PDB entry 1dte coloured by chain, side view.
PDB entry 1dte coloured by chain, top view.
Source organism: Thermomyces lanuginosus
Primary publication:
Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase.
Brzozowski AM, Savage H, Verma CS, Turkenburg JP, Lawson DM, Svendsen A, Patkar S
Biochemistry 39 15071-82 (2000)
PMID: 11106485

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129890 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipase Chains: A, B
Molecule details ›
Chains: A, B
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:
Structure domains: alpha/beta hydrolase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 96.127Å b: 71.096Å c: 82.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.263 0.263 0.352

Quick links

Citations

10 review citations

Modifying enzyme activity and selectivity by immobilization.
Rodrigues et al. (2013)
9 more

8 mentions without citation

Perspectives on the Role of Enzymatic Biocatalysis for the Degradation of Plastic PET.
Magalhães et al. (2021)
7 more