› 4lip

X-ray diffraction
1.75Å resolution

PSEUDOMONAS LIPASE COMPLEXED WITH RC-(RP, SP)-DIBUTYLCARBAMOYLGLYCERO-3-O-BUTYLPHOSPHONATE

Released:
DOI: 10.2210/pdb4lip/pdb
PDB entry 4lip coloured by chain, front view.
PDB entry 4lip coloured by chain, side view.
PDB entry 4lip coloured by chain, top view.
Source organism: Burkholderia cepacia
Primary publication:
Structural basis of the chiral selectivity of Pseudomonas cepacia lipase.
Lang DA, Mannesse ML, de Haas GH, Verheij HM, Dijkstra BW
Eur J Biochem 254 333-40 (1998)
PMID: 9660188

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 Chains: D, E
Molecule details ›
Chains: D, E
Length: 320 amino acids
Theoretical weight: 33.15 KDa
Source organism: Burkholderia cepacia
Expression system: Pseudomonas sp.
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

2 bound ligands:
Ligand CA 2 x CA
Ligand CCP 2 x CCP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: P21
Unit cell:
a: 84.04Å b: 46.36Å c: 85.38Å
α: 90° β: 116.53° γ: 90°
R-values:
R R work R free
0.178 0.178 0.202
Expression system: Pseudomonas sp.

Quick links

Citations

10 review citations

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

3 mentions without citation

Analysis of the distribution of functionally relevant rare codons.
Widmann et al. (2008)
2 more