› 1ein

X-ray diffraction
3Å resolution

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

Released:
DOI: 10.2210/pdb1ein/pdb
PDB entry 1ein coloured by chain, front view.
PDB entry 1ein coloured by chain, side view.
PDB entry 1ein 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, C
Molecule details ›
Chains: A, B, C
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

1 bound ligand:
Ligand PLC 3 x PLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P65
Unit cell:
a: 135.95Å b: 135.95Å c: 149.99Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.21 0.241

Quick links

Citations

9 review citations

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

8 mentions without citation

The Lid Domain in Lipases: Structural and Functional Determinant of Enzymatic Properties.
Khan et al. (2017)
7 more