Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE RAP A 225 |
| Chain | Residue |
| A | HOH11 |
| A | TRP175 |
| A | TYR198 |
| A | GLN203 |
| A | TYR135 |
| A | PHE145 |
| A | ASP146 |
| A | LEU162 |
| A | GLY169 |
| A | LYS170 |
| A | VAL171 |
| A | ILE172 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 96 |
| Details | Domain: {"description":"PPIase FKBP-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00277","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1d6o |
| Chain | Residue | Details |
| A | ILE172 | |
| A | TYR198 | |
| A | ASP146 | |
