› 3qyu

X-ray diffraction
1.54Å resolution

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

Released:
DOI: 10.2210/pdb3qyu/pdb
PDB entry 3qyu coloured by chain, front view.
PDB entry 3qyu coloured by chain, side view.
PDB entry 3qyu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
In-plate protein crystallization, in situ ligand soaking and X-ray diffraction.
le Maire A, Gelin M, Pochet S, Hoh F, Pirocchi M, Guichou JF, Ferrer JL, Labesse G
Acta Crystallogr D Biol Crystallogr 67 747-55 (2011)
PMID: 21904027

Function and Biology Details

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

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: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 17.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • 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-values:
R R work R free
0.151 0.148 0.189
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Protein X-ray Crystallography and Drug Discovery.
Maveyraud et al. (2020)
2 more

4 mentions without citation

Structural mechanisms of cyclophilin D-dependent control of the mitochondrial permeability transition pore.
Gutiérrez-Aguilar et al. (2015)
3 more