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› 1lpn

X-ray diffraction
2.18Å resolution

ANALOGS OF REACTION INTERMEDIATES IDENTIFY A UNIQUE SUBSTRATE BINDING SITE IN CANDIDA RUGOSA LIPASE

Released:
DOI: 10.2210/pdb1lpn/pdb
Model geometry
Fit model/data
PDB entry 1lpn coloured by chain, front view.
PDB entry 1lpn coloured by chain, side view.
PDB entry 1lpn coloured by chain, top view.
Source organism: Diutina rugosa
Primary publication:
Analogs of reaction intermediates identify a unique substrate binding site in Candida rugosa lipase.
Grochulski P, Bouthillier F, Kazlauskas RJ, Serreqi AN, Schrag JD, Ziomek E, Cygler M
Biochemistry 33 3494-500 (1994)
PMID: 8142346

Function and Biology Details

Reaction catalysed: 
a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+).
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-148911 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lipase 1 Chain: A
Molecule details ›
Chain: A
Length: 549 amino acids
Theoretical weight: 58.59 KDa
Source organism: Diutina rugosa
Expression system: Not provided
UniProt:
  • Canonical: P20261 (Residues: 1-549; Coverage: 100%)
Gene name: LIP1
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
3 bound ligands:
Ligand NAG 1 x NAG
Ligand CA 2 x CA
Ligand DSC 2 x DSC
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Spacegroup: C2221
Unit cell:
a: 65Å b: 97.4Å c: 176.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.151 not available
Expression system: Not provided

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Citations

22 review citations

Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases.
Jaeger et al. (1999)
21 more

6 mentions without citation

Towards the prediction of protein interaction partners using physical docking.
Wass et al. (2011)
5 more