5X9U
Crystal structure of group III chaperonin in the open state
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 | 0042802 | molecular_function | identical 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 | 0042802 | molecular_function | identical protein binding |
| B | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006457 | biological_process | protein folding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006457 | biological_process | protein folding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue ADP A 601 |
| Chain | Residue |
| A | PRO37 |
| A | MET430 |
| A | PHE461 |
| A | MET469 |
| A | VAL474 |
| A | ASP476 |
| A | ASP87 |
| A | GLY88 |
| A | THR89 |
| A | THR90 |
| A | THR91 |
| A | GLY389 |
| A | GLY390 |
| A | GLY391 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue ADP B 601 |
| Chain | Residue |
| B | PRO37 |
| B | ASP87 |
| B | GLY88 |
| B | THR89 |
| B | THR90 |
| B | THR91 |
| B | GLY389 |
| B | GLY390 |
| B | MET430 |
| B | MET469 |
| B | VAL474 |
| B | ASP476 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | binding site for residue ADP C 601 |
| Chain | Residue |
| C | PRO37 |
| C | ASP87 |
| C | GLY88 |
| C | THR90 |
| C | THR91 |
| C | ILE152 |
| C | GLY389 |
| C | GLY390 |
| C | MET430 |
| C | VAL474 |
| C | ASP476 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue ADP D 601 |
| Chain | Residue |
| D | PRO37 |
| D | ASP87 |
| D | GLY88 |
| D | THR89 |
| D | THR90 |
| D | THR91 |
| D | GLY389 |
| D | GLY390 |
| D | MET430 |
| D | MET469 |
| D | VAL474 |
| D | ASP476 |
Functional Information from PROSITE/UniProt
| site_id | PS00995 |
| Number of Residues | 9 |
| Details | TCP1_3 Chaperonins TCP-1 signature 3. QEreVGDGT |
| Chain | Residue | Details |
| A | GLN81-THR89 |
