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 | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006457 | biological_process | protein folding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR CHAIN B OF SUCCINYL-ALA-PRO-ALA-P-NITROANILIDE |
| Chain | Residue |
| A | ARG43 |
| A | SER93 |
| A | PHE99 |
| A | ASP106 |
| A | PHE107 |
| A | TYR120 |
| A | HOH277 |
| B | HOH299 |
| B | HOH349 |
| B | HOH354 |
| B | HOH355 |
| A | ILE45 |
| A | PHE48 |
| A | MET49 |
| A | ALA86 |
| A | ARG87 |
| A | THR88 |
| A | ALA90 |
| A | HIS92 |
Functional Information from PROSITE/UniProt
| site_id | PS00170 |
| Number of Residues | 18 |
| Details | CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YnnTiFHRVIngFMiQGG |
| Chain | Residue | Details |
| A | TYR36-GLY53 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 161 |
| Details | Domain: {"description":"PPIase cyclophilin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00156","evidenceCode":"ECO:0000255"}]} |
1LOP
