› 1dyw

X-ray diffraction
1.8Å resolution

Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans

Released:
DOI: 10.2210/pdb1dyw/pdb
PDB entry 1dyw coloured by chain, front view.
PDB entry 1dyw coloured by chain, side view.
PDB entry 1dyw coloured by chain, top view.
Source organism: Caenorhabditis elegans
Primary publication:
Biochemical and structural characterization of a divergent loop cyclophilin from Caenorhabditis elegans.
Dornan J, Page AP, Taylor P, Wu Sy, Winter AD, Husi H, Walkinshaw MD
J Biol Chem 274 34877-83 (1999)
PMID: 10574961

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156454 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase 3 Chain: A
Molecule details ›
Chain: A
Length: 173 amino acids
Theoretical weight: 18.58 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: P52011 (Residues: 1-173; Coverage: 100%)
Gene names: Y75B12B.5, cyn-3, cyp-3
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ENRAF-NONIUS FR571
Spacegroup: P41212
Unit cell:
a: 60.608Å b: 60.608Å c: 123.124Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 not available 0.286
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Peptidyl-prolyl cis-trans isomerases (immunophilins) and their roles in parasite biochemistry, host-parasite interaction and antiparasitic drug action.
Bell et al. (2006)
4 more

4 mentions without citation

Mapping the distribution of packing topologies within protein interiors shows predominant preference for specific packing motifs.
Basu et al. (2011)
3 more