PDBe 1dyw

X-ray diffraction
1.8Å resolution

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

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (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