PDBe 1w8l

X-ray diffraction
1.8Å 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: Escherichia coli
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

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NONIUS
Spacegroup: P212121
Unit cell:
a: 36.09Å b: 54.31Å c: 70.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.23
Expression system: Escherichia coli