› 1trh

X-ray diffraction
2.1Å resolution

TWO CONFORMATIONAL STATES OF CANDIDA RUGOSA LIPASE

Released:
DOI: 10.2210/pdb1trh/pdb
PDB entry 1trh coloured by chain, front view.
PDB entry 1trh coloured by chain, side view.
PDB entry 1trh coloured by chain, top view.
Source organism: Diutina rugosa
Primary publication:
Two conformational states of Candida rugosa lipase.
Grochulski P, Li Y, Schrag JD, Cygler M
Protein Sci 3 82-91 (1994)
PMID: 8142901

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-539436 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipase 1 Chain: A
Molecule details ›
Chain: A
Length: 534 amino acids
Theoretical weight: 57.13 KDa
Source organism: Diutina rugosa
Expression system: Not provided
UniProt:
  • Canonical: P20261 (Residues: 16-549; Coverage: 100%)
Gene name: LIP1
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand NAG 2 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 105Å b: 106.7Å c: 59.8Å
α: 90° β: 94.8° γ: 90°
R-values:
R R work R free
0.148 0.148 not available
Expression system: Not provided

Quick links

Citations

15 review citations

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

15 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)
14 more