› 2x25

X-ray diffraction
1.2Å resolution

Free acetyl-CypA orthorhombic form

Released:
DOI: 10.2210/pdb2x25/pdb
PDB entry 2x25 coloured by chain, front view.
PDB entry 2x25 coloured by chain, side view.
PDB entry 2x25 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization.
Lammers M, Neumann H, Chin JW, James LC
Nat Chem Biol 6 331-7 (2010)
PMID: 20364129

Function and Biology Details

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

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: B
Molecule details ›
Chain: B
Length: 169 amino acids
Theoretical weight: 18.64 KDa
Source organism: Homo sapiens
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

No bound ligands
1 modified residue:
Ligand ALY 1 x ALY

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 42.222Å b: 52.404Å c: 89.236Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.128 0.126 0.156

Quick links

Citations

26 review citations

The growing landscape of lysine acetylation links metabolism and cell signalling.
Choudhary et al. (2014)
25 more

5 mentions without citation

Acetylation regulates cyclophilin A catalysis, immunosuppression and HIV isomerization.
Lammers et al. (2010)
4 more