Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006457 | biological_process | protein folding |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0042026 | biological_process | protein refolding |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006457 | biological_process | protein folding |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0042026 | biological_process | protein refolding |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006457 | biological_process | protein folding |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0042026 | biological_process | protein refolding |
| C | 0051082 | molecular_function | unfolded protein binding |
| C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006457 | biological_process | protein folding |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0042026 | biological_process | protein refolding |
| D | 0051082 | molecular_function | unfolded protein binding |
| D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006457 | biological_process | protein folding |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0042026 | biological_process | protein refolding |
| E | 0051082 | molecular_function | unfolded protein binding |
| E | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006457 | biological_process | protein folding |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0042026 | biological_process | protein refolding |
| F | 0051082 | molecular_function | unfolded protein binding |
| F | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006457 | biological_process | protein folding |
| G | 0016853 | molecular_function | isomerase activity |
| G | 0042026 | biological_process | protein refolding |
| G | 0051082 | molecular_function | unfolded protein binding |
| G | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PROSITE/UniProt
| site_id | PS00296 |
| Number of Residues | 12 |
| Details | CHAPERONINS_CPN60 Chaperonins cpn60 signature. AAVQEGIVvGGG |
| Chain | Residue | Details |
| A | ALA405-GLY416 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | THR30 | |
| B | ASP496 | |
| C | THR30 | |
| C | LYS51 | |
| C | ASP87 | |
| C | GLY415 | |
| C | ASP496 | |
| D | THR30 | |
| D | LYS51 | |
| D | ASP87 | |
| D | GLY415 | |
| A | LYS51 | |
| D | ASP496 | |
| E | THR30 | |
| E | LYS51 | |
| E | ASP87 | |
| E | GLY415 | |
| E | ASP496 | |
| F | THR30 | |
| F | LYS51 | |
| F | ASP87 | |
| F | GLY415 | |
| A | ASP87 | |
| F | ASP496 | |
| G | THR30 | |
| G | LYS51 | |
| G | ASP87 | |
| G | GLY415 | |
| G | ASP496 | |
| A | GLY415 | |
| A | ASP496 | |
| B | THR30 | |
| B | LYS51 | |
| B | ASP87 | |
| B | GLY415 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| A | THR90 | |
| A | ASP52 | |
| A | ASP398 | |
| A | THR89 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| B | THR90 | |
| B | ASP52 | |
| B | ASP398 | |
| B | THR89 | |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| C | THR90 | |
| C | ASP52 | |
| C | ASP398 | |
| C | THR89 | |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| D | THR90 | |
| D | ASP52 | |
| D | ASP398 | |
| D | THR89 | |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| E | THR90 | |
| E | ASP52 | |
| E | ASP398 | |
| E | THR89 | |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| F | THR90 | |
| F | ASP52 | |
| F | ASP398 | |
| F | THR89 | |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1q3q |
| Chain | Residue | Details |
| G | THR90 | |
| G | ASP52 | |
| G | ASP398 | |
| G | THR89 | |
