PDBe 1w8v

X-ray diffraction
1.7Å resolution

Enzymatic and structural characterization of non peptide ligand cyclophilin complexes

Released:
Source organism: Homo sapiens
Primary publication:
Enzymatic and structural characterization of non-peptide ligand-cyclophilin complexes.
Acta Crystallogr. D Biol. Crystallogr. 60 479-85 (2004)
PMID: 14993672

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase A Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.04 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P62937 (Residues: 1-165; Coverage: 100%)
Gene names: CYPA, PPIA
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: NONIUS
Spacegroup: P212121
Unit cell:
a: 36.182Å b: 56.593Å c: 70.239Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.174 0.219
Expression system: Not provided