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 | 0006457 | biological_process | protein folding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 53Z A 301 |
Chain | Residue |
A | ARG97 |
A | GLN153 |
A | PHE155 |
A | HIS168 |
A | HOH477 |
A | HOH497 |
A | HOH618 |
A | PHE102 |
A | MET103 |
A | GLN105 |
A | GLY114 |
A | ARG124 |
A | ALA143 |
A | ASN144 |
A | THR149 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE PO4 A 302 |
Chain | Residue |
A | LEU164 |
A | LYS167 |
A | HIS168 |
A | HOH521 |
A | HOH599 |
A | HOH717 |
A | HOH735 |
Functional Information from PROSITE/UniProt
site_id | PS00170 |
Number of Residues | 18 |
Details | CSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgStFHRVIpsFMcQAG |
Chain | Residue | Details |
A | TYR90-GLY107 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LYS67 | |
Chain | Residue | Details |
A | LYS86 | |
A | ILE175 | |
A | LYS190 | |
Chain | Residue | Details |
A | LYS167 | |
Chain | Residue | Details |
A | CYS203 | |