› 2cyh

X-ray diffraction
1.64Å resolution

CYCLOPHILIN A COMPLEXED WITH DIPEPTIDE ALA-PRO

Released:
DOI: 10.2210/pdb2cyh/pdb
PDB entry 2cyh coloured by chain, front view.
PDB entry 2cyh coloured by chain, side view.
PDB entry 2cyh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mechanistic implication of crystal structures of the cyclophilin-dipeptide complexes.
Zhao Y, Ke H
Biochemistry 35 7362-8 (1996)
PMID: 8652512

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158766 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase A Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 17.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62937 (Residues: 2-165; Coverage: 99%)
Gene names: CYPA, PPIA
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

2 bound ligands:
Ligand ALA 1 x ALA
Ligand PRO 1 x PRO
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 40.7Å b: 52.3Å c: 90.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Immunophilins: switched on protein binding domains?
Ivery MT. (2000)
1 more

3 mentions without citation

BP-Dock: a flexible docking scheme for exploring protein-ligand interactions based on unbound structures.
Bolia et al. (2014)
2 more