7R9M
Methanococcus maripaludis chaperonin, closed conformation 2
Functional Information from GO Data
Chain | GOid | namespace | contents |
J | 0005524 | molecular_function | ATP binding |
J | 0006457 | biological_process | protein folding |
J | 0016887 | molecular_function | ATP hydrolysis activity |
J | 0042802 | molecular_function | identical protein binding |
J | 0046872 | molecular_function | metal ion binding |
J | 0051082 | molecular_function | unfolded protein binding |
J | 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. RStLGPkGmdKML |
Chain | Residue | Details |
J | ARG36-LEU48 |
site_id | PS00751 |
Number of Residues | 17 |
Details | TCP1_2 Chaperonins TCP-1 signature 2. VTNDGVTILreMsVeHP |
Chain | Residue | Details |
J | VAL57-PRO73 |
site_id | PS00995 |
Number of Residues | 9 |
Details | TCP1_3 Chaperonins TCP-1 signature 3. QEkeVGDGT |
Chain | Residue | Details |
J | GLN85-THR93 |