› 1ys2

X-ray diffraction
1.5Å resolution

Burkholderia cepacia lipase complexed with hexylphosphonic acid (S) 2-methyl-3-phenylpropyl ester

Released:
DOI: 10.2210/pdb1ys2/pdb
PDB entry 1ys2 coloured by chain, front view.
PDB entry 1ys2 coloured by chain, side view.
PDB entry 1ys2 coloured by chain, top view.
Source organism: Burkholderia cepacia
Primary publication:
Mirror-image packing in enantiomer discrimination molecular basis for the enantioselectivity of B.cepacia lipase toward 2-methyl-3-phenyl-1-propanol.
Mezzetti A, Schrag JD, Cheong CS, Kazlauskas RJ
Chem Biol 12 427-37 (2005)
PMID: 15850979

Function and Biology Details

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

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: X
Molecule details ›
Chain: X
Length: 320 amino acids
Theoretical weight: 33.06 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

2 bound ligands:
Ligand CA 1 x CA
Ligand 2HS 1 x 2HS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: C2
Unit cell:
a: 88.93Å b: 46.233Å c: 84.729Å
α: 90° β: 121.35° γ: 90°
R-values:
R R work R free
0.151 0.151 0.162

Quick links

Citations

3 review citations

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

4 mentions without citation

Modelling substrate specificity and enantioselectivity for lipases and esterases by substrate-imprinted docking.
Juhl et al. (2009)
3 more