Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006457 | biological_process | protein folding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006457 | biological_process | protein folding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PROSITE/UniProt
| site_id | PS00750 |
| Number of Residues | 13 |
| Details | TCP1_1 Chaperonins TCP-1 signature 1. RSsLGPrGmdKML |
| Chain | Residue | Details |
| B | ARG38-LEU50 | |
| A | ARG39-LEU51 | |
| site_id | PS00751 |
| Number of Residues | 17 |
| Details | TCP1_2 Chaperonins TCP-1 signature 2. ITNDGVTILkeMdVeHP |
| Chain | Residue | Details |
| B | ILE59-PRO75 | |
| A | ILE60-PRO76 | |
| site_id | PS00995 |
| Number of Residues | 9 |
| Details | TCP1_3 Chaperonins TCP-1 signature 3. QDsfVGDGT |
| Chain | Residue | Details |
| B | GLN87-THR95 | |
| A | GLN88-THR96 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 9546398 |
| Chain | Residue | Details |
| A | THR97 | |
| A | ASP390 | |
| A | THR96 | |
| A | ASP63 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 9546398 |
| Chain | Residue | Details |
| B | ASP391 | |
| B | THR95 | |
| B | ASP62 | |
| B | THR96 | |
