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 | 9 |
Details | BINDING SITE FOR RESIDUE JZI A 301 |
Chain | Residue |
A | HIS59 |
A | LEU61 |
A | LYS63 |
A | CYS113 |
A | SER114 |
A | LEU122 |
A | PHE134 |
A | SER154 |
A | HIS157 |
site_id | AC2 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE JZI B 302 |
Chain | Residue |
B | HOH2 |
B | HIS59 |
B | LEU61 |
B | LYS63 |
B | ARG68 |
B | ARG69 |
B | ARG69 |
B | CYS113 |
B | SER114 |
B | LEU122 |
B | PHE134 |
B | SER154 |
B | HIS157 |
B | HOH177 |
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
Chain | Residue | Details |
A | LYS46 | |
B | LYS46 | |
Chain | Residue | Details |
A | SER71 | |
B | SER71 | |
Chain | Residue | Details |
A | SER108 | |
B | SER108 | |
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 |