› 2bit

X-ray diffraction
1.71Å resolution

Crystal structure of human cyclophilin D at 1.7 A resolution

Released:
DOI: 10.2210/pdb2bit/pdb
PDB entry 2bit coloured by chain, front view.
PDB entry 2bit coloured by chain, side view.
PDB entry 2bit coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal engineering yields crystals of cyclophilin D diffracting to 1.7 A resolution.
Schlatter D, Thoma R, Küng E, Stihle M, Müller F, Borroni E, Cesura A, Hennig M
Acta Crystallogr D Biol Crystallogr 61 513-9 (2005)
PMID: 15858260

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151715 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase F, mitochondrial Chain: X
Molecule details ›
Chain: X
Length: 165 amino acids
Theoretical weight: 17.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P30405 (Residues: 43-207; Coverage: 80%)
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: NONIUS
Spacegroup: P41212
Unit cell:
a: 57.165Å b: 57.165Å c: 87.227Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.141 0.139 0.175
Expression system: Escherichia coli

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Citations

4 review citations

The permeability transition pore in cell death.
Grimm et al. (2007)
3 more

14 mentions without citation

Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases.
Davis et al. (2010)
13 more