› 2nw6

X-ray diffraction
1.8Å resolution

Burkholderia cepacia lipase complexed with S-inhibitor

Released:
DOI: 10.2210/pdb2nw6/pdb
PDB entry 2nw6 coloured by chain, front view.
PDB entry 2nw6 coloured by chain, side view.
PDB entry 2nw6 coloured by chain, top view.
Source organism: Burkholderia cepacia
Primary publication:
Combined X-ray diffraction and QM/MM study of the Burkholderia cepacia lipase-catalyzed secondary alcohol esterification.
Luić M, Stefanić Z, Ceilinger I, Hodoscek M, Janezic D, Lenac T, Asler IL, Sepac D, Tomić S
J Phys Chem B 112 4876-83 (2008)
PMID: 18386861

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

3 bound ligands:
Ligand CA 1 x CA
Ligand NA 1 x NA
Ligand POT 1 x POT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 89.015Å b: 46.584Å c: 84.244Å
α: 90° β: 121.05° γ: 90°
R-values:
R R work R free
0.185 0.175 0.213

Quick links

Citations

1 review citation

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

4 mentions without citation

BioGPS descriptors for rational engineering of enzyme promiscuity and structure based bioinformatic analysis.
Ferrario et al. (2014)
3 more