8B58
Crystal Structure of Cyclophilin TgCyp23 from Toxoplasma gondii in complex with Cyclosporin A
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 | 0005737 | cellular_component | cytoplasm |
| A | 0006457 | biological_process | protein folding |
| A | 0016018 | molecular_function | cyclosporin A binding |
| A | 0016853 | molecular_function | isomerase activity |
| B | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| B | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006457 | biological_process | protein folding |
| B | 0016018 | molecular_function | cyclosporin A binding |
| B | 0016853 | molecular_function | isomerase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00170 |
| Number of Residues | 18 |
| Details | CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgAtFHRIIknFMiQGG |
| Chain | Residue | Details |
| A | TYR92-GLY109 |






