› 2x2a

X-ray diffraction
1.4Å resolution

Free acetyl-CypA trigonal form

Released:
DOI: 10.2210/pdb2x2a/pdb
PDB entry 2x2a coloured by chain, front view.
PDB entry 2x2a coloured by chain, side view.
PDB entry 2x2a 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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158803 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 165 amino acids
Theoretical weight: 18.08 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P62937 (Residues: 1-165; Coverage: 100%)
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 GOL 1 x GOL
Ligand SO4 2 x SO4
1 modified residue:
Ligand ALY 2 x ALY

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 64.3Å b: 64.3Å c: 173.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.125 0.123 0.161

Quick links

Citations

26 review citations

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

2 mentions without citation

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