› 1tgl

X-ray diffraction
1.9Å resolution

A SERINE PROTEASE TRIAD FORMS THE CATALYTIC CENTRE OF A TRIACYLGLYCEROL LIPASE

Released:
DOI: 10.2210/pdb1tgl/pdb
PDB entry 1tgl coloured by chain, front view.
PDB entry 1tgl coloured by chain, side view.
PDB entry 1tgl coloured by chain, top view.
Source organism: Rhizomucor miehei
Primary publication:
A serine protease triad forms the catalytic centre of a triacylglycerol lipase.
Brady L, Brzozowski AM, Derewenda ZS, Dodson E, Dodson G, Tolley S, Turkenburg JP, Christiansen L, Huge-Jensen B, Norskov L
Nature 343 767-70 (1990)
PMID: 2304552

Function and Biology Details

Reaction catalysed: 
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148621 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipase Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 29.51 KDa
Source organism: Rhizomucor miehei
Expression system: Not provided
UniProt:
  • Canonical: P19515 (Residues: 95-363; Coverage: 79%)
Sequence domains: Lipase (class 3)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 71.6Å b: 75Å c: 55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.138 not available not available
Expression system: Not provided

Quick links

Citations

56 review citations

Molecular and cellular biology of cholinesterases.
Massoulié et al. (1993)
55 more

5 mentions without citation

Carboxylic ester hydrolases: Classification and database derived from their primary, secondary, and tertiary structures.
Chen et al. (2016)
4 more