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 | 3 |
Details | binding site for residue EDO A 201 |
Chain | Residue |
A | ASN13 |
A | LYS15 |
A | LYS154 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 202 |
Chain | Residue |
A | GLN163 |
A | SER165 |
A | EDO203 |
A | HOH302 |
A | HOH377 |
A | HOH419 |
site_id | AC3 |
Number of Residues | 2 |
Details | binding site for residue EDO A 203 |
Chain | Residue |
A | GLN163 |
A | EDO202 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 204 |
Chain | Residue |
A | ARG19 |
A | GLU134 |
A | LEU164 |
A | HOH395 |
A | HOH412 |
site_id | AC5 |
Number of Residues | 7 |
Details | binding site for residue EDO A 205 |
Chain | Residue |
A | LYS31 |
A | GLU134 |
A | GLY135 |
A | ASP137 |
A | HOH305 |
A | HOH356 |
A | HOH369 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue 12P A 206 |
Chain | Residue |
A | ILE78 |
A | VAL93 |
A | PRO95 |
A | HIS131 |
A | HOH337 |
A | HOH387 |
A | HOH407 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue 12P A 207 |
Chain | Residue |
A | GLY50 |
A | LYS155 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue PO4 A 208 |
Chain | Residue |
A | SER147 |
A | LYS148 |
A | HOH304 |
A | HOH319 |
A | HOH321 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue NA A 209 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue NA A 211 |
Chain | Residue |
A | GLY80 |
A | SER81 |
A | HOH320 |
A | HOH359 |
A | HOH414 |
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 | TYR48-GLY65 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LYS25 | |
Chain | Residue | Details |
A | LYS44 | |
A | ILE133 | |
A | LYS148 | |
Chain | Residue | Details |
A | LYS125 | |
Chain | Residue | Details |
A | CYS161 | |