› 3lip

X-ray diffraction
2Å resolution

OPEN CONFORMATION OF PSEUDOMONAS CEPACIA LIPASE

Released:
DOI: 10.2210/pdb3lip/pdb
PDB entry 3lip coloured by chain, front view.
PDB entry 3lip coloured by chain, side view.
PDB entry 3lip coloured by chain, top view.
Source organism: Burkholderia cepacia
Primary publication:
The open conformation of a Pseudomonas lipase.
Schrag JD, Li Y, Cygler M, Lang D, Burgdorf T, Hecht HJ, Schmid R, Schomburg D, Rydel TJ, Oliver JD, Strickland LC, Dunaway CM, Larson SB, Day J, McPherson A
Structure 5 187-202 (1997)
PMID: 9032074

Function and Biology Details

Reaction catalysed: 
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149521 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triacylglycerol lipase Chain: A
Molecule details ›
Chain: A
Length: 320 amino acids
Theoretical weight: 33.15 KDa
Source organism: Burkholderia cepacia
UniProt:
  • Canonical: P22088 (Residues: 45-364; Coverage: 100%)
Gene names: lip, lipA
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: C2
Unit cell:
a: 91.3Å b: 47.3Å c: 85.4Å
α: 90° β: 121.4° γ: 90°
R-values:
R R work R free
0.188 0.188 not available

Quick links

Citations

13 review citations

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

11 mentions without citation

Secondary-structure analysis of denatured proteins by vacuum-ultraviolet circular dichroism spectroscopy.
Matsuo et al. (2007)
10 more