› 4o8i

X-ray diffraction
1.45Å resolution

1.45A resolution structure of PEG 400 Bound Cyclophilin D

Released:
DOI: 10.2210/pdb4o8i/pdb
PDB entry 4o8i coloured by chain, front view.
PDB entry 4o8i coloured by chain, side view.
PDB entry 4o8i coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
High-resolution crystal structures of two crystal forms of human cyclophilin D in complex with PEG 400 molecules.
Valasani KR, Carlson EA, Battaile KP, Bisson A, Wang C, Lovell S, ShiDu Yan S
Acta Crystallogr F Struct Biol Commun 70 717-22 (2014)
PMID: 24915078

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: 165 amino acids
Theoretical weight: 17.74 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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

1 bound ligand:
Ligand 1PE 1 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 40.564Å b: 57.011Å c: 57.336Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.16 0.19
Expression system: Escherichia coli BL21(DE3)

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Citations

1 citations in other articles

Selective Inhibition of the Mitochondrial Permeability Transition Pore Protects against Neurodegeneration in Experimental Multiple Sclerosis.
Warne et al. (2016)

1 mention without citation

High-resolution crystal structures of two crystal forms of human cyclophilin D in complex with PEG 400 molecules.
Valasani et al. (2014)