› 1cle

X-ray diffraction
2Å resolution

STRUCTURE OF UNCOMPLEXED AND LINOLEATE-BOUND CANDIDA CYLINDRACEA CHOLESTEROL ESTERASE

Released:
DOI: 10.2210/pdb1cle/pdb
PDB entry 1cle coloured by chain, front view.
PDB entry 1cle coloured by chain, side view.
PDB entry 1cle coloured by chain, top view.
Source organism: Limtongozyma cylindracea
Primary publication:
Structure of uncomplexed and linoleate-bound Candida cylindracea cholesterol esterase.
Ghosh D, Wawrzak Z, Pletnev VZ, Li N, Kaiser R, Pangborn W, Jörnvall H, Erman M, Duax WL
Structure 3 279-88 (1995)
PMID: 7788294

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-542938 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Lipase 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 534 amino acids
Theoretical weight: 57.33 KDa
Source organism: Limtongozyma cylindracea
UniProt:
  • Canonical: P32947 (Residues: 16-549; Coverage: 100%)
Gene name: LIP3
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
3 bound ligands:
Ligand NAG 2 x NAG
Ligand PO4 2 x PO4
Ligand CLL 2 x CLL
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P1
Unit cell:
a: 58.79Å b: 90.92Å c: 58.79Å
α: 93.39° β: 105.74° γ: 97.22°
R-values:
R R work R free
0.149 0.149 not available

Quick links

Citations

9 review citations

Structure-activity of cutinase, a small lipolytic enzyme.
Longhi et al. (1999)
8 more

9 mentions without citation

LIGSITEcsc: predicting ligand binding sites using the Connolly surface and degree of conservation.
Huang et al. (2006)
8 more