› 4tgl

X-ray diffraction
2.6Å resolution

CATALYSIS AT THE INTERFACE: THE ANATOMY OF A CONFORMATIONAL CHANGE IN A TRIGLYCERIDE LIPASE

Released:
DOI: 10.2210/pdb4tgl/pdb
PDB entry 4tgl coloured by chain, front view.
PDB entry 4tgl coloured by chain, side view.
PDB entry 4tgl coloured by chain, top view.
Source organism: Rhizomucor miehei
Primary publication:
Catalysis at the interface: the anatomy of a conformational change in a triglyceride lipase.
Derewenda U, Brzozowski AM, Lawson DM, Derewenda ZS
Biochemistry 31 1532-41 (1992)
PMID: 1737010

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: 29.52 KDa
Source organism: Rhizomucor miehei
Expression system: Not provided
UniProt:
  • Canonical: P19515 (Residues: 95-363; Coverage: 79%)
Sequence domains: Lipase (class 3)
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand DEP 1 x DEP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 48.3Å b: 93.9Å c: 122.1Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.129 not available not available
Expression system: Not provided

Quick links

Citations

26 review citations

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

33 mentions without citation

Recognition of functional sites in protein structures.
Shulman-Peleg et al. (2004)
32 more