Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003755 | molecular_function | peptidyl-prolyl cis-trans isomerase activity |
| B | 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 39X A 201 |
| Chain | Residue |
| A | HIS59 |
| A | SER154 |
| A | HIS157 |
| A | HOH312 |
| A | LEU61 |
| A | LYS63 |
| A | CYS113 |
| A | SER114 |
| A | SER115 |
| A | LEU122 |
| A | GLN131 |
| A | PHE134 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 202 |
| Chain | Residue |
| A | THR79 |
| A | GLU84 |
| A | VAL150 |
| A | PHE151 |
| A | HOH303 |
| A | HOH314 |
| A | HOH375 |
| site_id | AC3 |
| Number of Residues | 17 |
| Details | binding site for residue 39X B 201 |
| Chain | Residue |
| B | HIS59 |
| B | LEU61 |
| B | LYS63 |
| B | ARG68 |
| B | ARG69 |
| B | ARG69 |
| B | CYS113 |
| B | SER114 |
| B | SER115 |
| B | LEU122 |
| B | GLN131 |
| B | PHE134 |
| B | SER154 |
| B | GOL202 |
| B | HOH307 |
| B | HOH318 |
| B | HOH341 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue GOL B 202 |
| Chain | Residue |
| B | ARG68 |
| B | GLN129 |
| B | GLN131 |
| B | GLN131 |
| B | 39X201 |
| B | HOH303 |
| B | HOH307 |
| B | HOH309 |
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 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 222 |
| Details | Domain: {"description":"PpiC","evidences":[{"source":"PROSITE-ProRule","id":"PRU00278","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by DAPK1","evidences":[{"source":"PubMed","id":"21497122","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29686383","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"}]} |
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 |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 511 |
| Chain | Residue | Details |
| B | HIS59 | proton shuttle (general acid/base) |
| B | CYS113 | covalently attached, electrostatic stabiliser |
| B | GLN131 | electrostatic stabiliser |
| B | SER154 | electrostatic stabiliser |
| B | HIS157 | electrostatic stabiliser |
