› 1hqd

X-ray diffraction
2.3Å resolution

PSEUDOMONAS CEPACIA LIPASE COMPLEXED WITH TRANSITION STATE ANALOGUE OF 1-PHENOXY-2-ACETOXY BUTANE

Released:
DOI: 10.2210/pdb1hqd/pdb
PDB entry 1hqd coloured by chain, front view.
PDB entry 1hqd coloured by chain, side view.
PDB entry 1hqd coloured by chain, top view.
Source organism: Burkholderia cepacia
Primary publication:
Complex of Burkholderia cepacia lipase with transition state analogue of 1-phenoxy-2-acetoxybutane: biocatalytic, structural and modelling study.
Luić M, Tomić S, Lescić I, Ljubović E, Sepac D, Sunjić V, Vitale L, Saenger W, Kojic-Prodić B
Eur J Biochem 268 3964-73 (2001)
PMID: 11453990

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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 89.06Å b: 46.63Å c: 84.3Å
α: 90° β: 120.86° γ: 90°
R-values:
R R work R free
0.154 0.154 0.203

Quick links

Citations

2 review citations

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

6 mentions without citation

How the Same Core Catalytic Machinery Catalyzes 17 Different Reactions: the Serine-Histidine-Aspartate Catalytic Triad of α/β-Hydrolase Fold Enzymes.
Rauwerdink et al. (2015)
5 more