Functional Information from PROSITE/UniProt
| site_id | PS01096 |
| Number of Residues | 21 |
| Details | PPIC_PPIASE_1 PpiC-type peptidyl-prolyl cis-trans isomerase signature. FEsLAsqfSdcs.Saka..RGdLG |
| Chain | Residue | Details |
| A | PHE103-GLY123 |
| site_id | PS01159 |
| Number of Residues | 27 |
| Details | WW_DOMAIN_1 WW/rsp5/WWP domain signature. WekamsrssgrvYYfnhitnaSQWERP |
| Chain | Residue | Details |
| A | TRP11-PRO37 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 111 |
| Details | Domain: {"description":"PpiC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00278","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by DAPK1","evidences":[{"source":"PubMed","id":"21497122","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29686383","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 511 |
| Chain | Residue | Details |
| A | HIS59 | proton shuttle (general acid/base) |
| A | CYS113 | covalently attached, electrostatic stabiliser |
| A | GLN131 | electrostatic stabiliser |
| A | SER154 | electrostatic stabiliser |
| A | HIS157 | electrostatic stabiliser |
