› 1tah

X-ray diffraction
3Å resolution

THE CRYSTAL STRUCTURE OF TRIACYLGLYCEROL LIPASE FROM PSEUDOMONAS GLUMAE REVEALS A PARTIALLY REDUNDANT CATALYTIC ASPARTATE

Released:
DOI: 10.2210/pdb1tah/pdb
PDB entry 1tah coloured by chain, front view.
PDB entry 1tah coloured by chain, side view.
PDB entry 1tah coloured by chain, top view.
Source organism: Burkholderia glumae
Primary publication:
The crystal structure of triacylglycerol lipase from Pseudomonas glumae reveals a partially redundant catalytic aspartate.
Noble ME, Cleasby A, Johnson LN, Egmond MR, Frenken LG
FEBS Lett 331 123-8 (1993)
PMID: 8405390

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-145126 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Triacylglycerol lipase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 318 amino acids
Theoretical weight: 33.05 KDa
Source organism: Burkholderia glumae
Expression system: Not provided
UniProt:
  • Canonical: P0DUB8 (Residues: 41-358; 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 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 158.16Å b: 158.64Å c: 63.36Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.159 0.226
Expression system: Not provided

Quick links

Citations

13 review citations

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

4 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
3 more