› 1lpm

X-ray diffraction
2.18Å resolution

A STRUCTURAL BASIS FOR THE CHIRAL PREFERENCES OF LIPASES

Released:
DOI: 10.2210/pdb1lpm/pdb
PDB entry 1lpm coloured by chain, front view.
PDB entry 1lpm coloured by chain, side view.
PDB entry 1lpm coloured by chain, top view.
Source organism: Diutina rugosa
Primary publication:
A Structural Basis for the Chiral Preferences of Lipases
Cygler M, Grochulski P, Kazlauskas RJ, Schrag JD, Bouthillier F, Rubin B, Serregi AN, Gupta AK
J. Am. Chem. Soc. 116 3180-3186 (1994)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
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 MPA 1 x MPA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 65.2Å b: 97.5Å c: 176.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.139 0.139 not available
Expression system: Not provided

Quick links

Citations

4 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
3 more