1Z81
Crystal Structure of cyclophilin from Plasmodium yoelii.
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
A | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006457 | biological_process | protein folding |
A | 0016853 | molecular_function | isomerase activity |
A | 0043231 | cellular_component | intracellular membrane-bounded organelle |
Functional Information from PROSITE/UniProt
site_id | PS00170 |
Number of Residues | 18 |
Details | CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YknTiFHRVIkeFMiQGG |
Chain | Residue | Details |
A | TYR90-GLY107 |