3KFK
Crystal structures of a group II chaperonin from Methanococcus maripaludis
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 | 0046872 | molecular_function | metal ion binding |
| 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 | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051082 | molecular_function | unfolded 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 | 0046872 | molecular_function | metal ion binding |
| C | 0051082 | molecular_function | unfolded 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 | 0046872 | molecular_function | metal ion binding |
| D | 0051082 | molecular_function | unfolded protein binding |
| D | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AGS A 544 |
| Chain | Residue |
| A | THR38 |
| A | THR95 |
| A | GLY403 |
| A | GLY404 |
| A | LEU473 |
| A | ASN474 |
| A | PHE476 |
| A | GLU490 |
| A | LEU39 |
| A | GLY40 |
| A | PRO41 |
| A | ASP60 |
| A | GLY61 |
| A | ASP91 |
| A | THR93 |
| A | THR94 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AGS B 544 |
| Chain | Residue |
| B | THR38 |
| B | LEU39 |
| B | GLY40 |
| B | PRO41 |
| B | ASP60 |
| B | GLY61 |
| B | ASP91 |
| B | GLY92 |
| B | THR93 |
| B | THR94 |
| B | THR95 |
| B | GLY403 |
| B | GLY404 |
| B | LEU473 |
| B | GLU490 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AGS C 544 |
| Chain | Residue |
| C | THR38 |
| C | LEU39 |
| C | GLY40 |
| C | PRO41 |
| C | ASP60 |
| C | GLY61 |
| C | ASP91 |
| C | GLY92 |
| C | THR93 |
| C | THR94 |
| C | THR95 |
| C | GLY403 |
| C | GLY404 |
| C | LEU473 |
| C | GLU490 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE AGS D 544 |
| Chain | Residue |
| D | GLY40 |
| D | ASP60 |
| D | ASP91 |
| D | GLY92 |
| D | THR93 |
| D | THR94 |
| D | THR95 |
| D | GLY403 |
| D | GLY404 |
| D | LEU473 |
| D | ASN474 |
| D | VAL488 |
| D | GLU490 |
Functional Information from PROSITE/UniProt
| site_id | PS00750 |
| Number of Residues | 13 |
| Details | TCP1_1 Chaperonins TCP-1 signature 1. RStLGPkGmdKML |
| Chain | Residue | Details |
| A | ARG36-LEU48 |
| site_id | PS00751 |
| Number of Residues | 17 |
| Details | TCP1_2 Chaperonins TCP-1 signature 2. VTNDGVTILreMsVeHP |
| Chain | Residue | Details |
| A | VAL57-PRO73 |
| site_id | PS00995 |
| Number of Residues | 9 |
| Details | TCP1_3 Chaperonins TCP-1 signature 3. QEkeVGDGT |
| Chain | Residue | Details |
| A | GLN85-THR93 |
