8CU5
Crystal Structure of Putative Cyclophilin B from Brugia malayi
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 | 0006457 | biological_process | protein folding |
| B | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| B | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| B | 0006457 | biological_process | protein folding |
| C | 0000413 | biological_process | protein peptidyl-prolyl isomerization |
| C | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| C | 0006457 | biological_process | protein folding |
Functional Information from PROSITE/UniProt
| site_id | PS00170 |
| Number of Residues | 18 |
| Details | CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgSkFHRVIkdFMiQGG |
| Chain | Residue | Details |
| A | TYR72-GLY89 |






