X-ray diffraction
1.54Å resolution

Crystal structure of human cyclophilin D at 1.54 A resolution at room temperature

Source organism: Homo sapiens
Primary publication:
In-plate protein crystallization, in situ ligand soaking and X-ray diffraction.
Acta Crystallogr. D Biol. Crystallogr. 67 747-55 (2011)
PMID: 21904027

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Peptidyl-prolyl cis-trans isomerase F, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 17.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P30405 (Residues: 44-207; Coverage: 79%)
Gene names: CYP3, PPIF
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: ESRF BEAMLINE BM30A, null
Spacegroup: P41212
Unit cell:
a: 57.927Å b: 57.927Å c: 88.537Å
α: 90° β: 90° γ: 90°
R R work R free
0.151 0.148 0.189
Expression system: Escherichia coli