3KFE
Crystal structures of a group II chaperonin from Methanococcus maripaludis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006457 | biological_process | protein folding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0032991 | cellular_component | protein-containing complex |
| 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 | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006457 | biological_process | protein folding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0032991 | cellular_component | protein-containing complex |
| 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 | 0000166 | molecular_function | nucleotide binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006457 | biological_process | protein folding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0032991 | cellular_component | protein-containing complex |
| 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 | 0000166 | molecular_function | nucleotide binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006457 | biological_process | protein folding |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0032991 | cellular_component | protein-containing complex |
| 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 |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006457 | biological_process | protein folding |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0032991 | cellular_component | protein-containing complex |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0051082 | molecular_function | unfolded protein binding |
| E | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006457 | biological_process | protein folding |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0032991 | cellular_component | protein-containing complex |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051082 | molecular_function | unfolded protein binding |
| F | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006457 | biological_process | protein folding |
| G | 0016887 | molecular_function | ATP hydrolysis activity |
| G | 0032991 | cellular_component | protein-containing complex |
| G | 0042802 | molecular_function | identical protein binding |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0051082 | molecular_function | unfolded protein binding |
| G | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0005524 | molecular_function | ATP binding |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006457 | biological_process | protein folding |
| H | 0016887 | molecular_function | ATP hydrolysis activity |
| H | 0032991 | cellular_component | protein-containing complex |
| H | 0042802 | molecular_function | identical protein binding |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0051082 | molecular_function | unfolded protein binding |
| H | 0140662 | molecular_function | ATP-dependent protein folding chaperone |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 544 |
| Chain | Residue |
| A | ASP91 |
| A | SER157 |
| A | LYS161 |
| A | ASP386 |
| A | ADP545 |
| A | SO4546 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP A 545 |
| Chain | Residue |
| A | ASP91 |
| A | GLY92 |
| A | THR93 |
| A | THR94 |
| A | THR95 |
| A | GLY160 |
| A | GLY404 |
| A | LEU473 |
| A | GLU490 |
| A | MG544 |
| A | SO4546 |
| A | THR38 |
| A | GLY40 |
| A | ASN59 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 A 546 |
| Chain | Residue |
| A | ASP60 |
| A | GLY61 |
| A | ASP91 |
| A | GLY92 |
| A | THR93 |
| A | THR94 |
| A | LYS161 |
| A | ASP386 |
| A | MG544 |
| A | ADP545 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 544 |
| Chain | Residue |
| B | ASP91 |
| B | SER157 |
| B | LYS161 |
| B | ASP386 |
| B | ADP545 |
| B | SO4546 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP B 545 |
| Chain | Residue |
| B | THR38 |
| B | GLY40 |
| B | ASN59 |
| B | ASP91 |
| B | GLY92 |
| B | THR93 |
| B | THR94 |
| B | THR95 |
| B | GLY160 |
| B | GLY404 |
| B | LEU473 |
| B | GLU490 |
| B | MG544 |
| B | SO4546 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 B 546 |
| Chain | Residue |
| B | ASP60 |
| B | GLY61 |
| B | ASP91 |
| B | GLY92 |
| B | THR93 |
| B | THR94 |
| B | LYS161 |
| B | ASP386 |
| B | MG544 |
| B | ADP545 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 544 |
| Chain | Residue |
| C | ASP91 |
| C | SER157 |
| C | ASP386 |
| C | ADP545 |
| C | SO4546 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ADP C 545 |
| Chain | Residue |
| C | THR38 |
| C | GLY40 |
| C | ASN59 |
| C | ASP91 |
| C | GLY92 |
| C | THR93 |
| C | THR94 |
| C | THR95 |
| C | GLY160 |
| C | GLY404 |
| C | LEU473 |
| C | GLU490 |
| C | MG544 |
| C | SO4546 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 C 546 |
| Chain | Residue |
| C | ASP60 |
| C | GLY61 |
| C | ASP91 |
| C | GLY92 |
| C | THR93 |
| C | THR94 |
| C | LYS161 |
| C | ASP386 |
| C | MG544 |
| C | ADP545 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 544 |
| Chain | Residue |
| D | ASP91 |
| D | SER157 |
| D | LYS161 |
| D | ASP386 |
| D | ADP545 |
| D | SO4546 |
| site_id | BC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADP D 545 |
| Chain | Residue |
| D | GLY92 |
| D | THR93 |
| D | THR94 |
| D | THR95 |
| D | GLY160 |
| D | GLY403 |
| D | GLY404 |
| D | LEU473 |
| D | GLU490 |
| D | MG544 |
| D | SO4546 |
| D | THR38 |
| D | GLY40 |
| D | ASN59 |
| D | ASP91 |
| site_id | BC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 D 546 |
| Chain | Residue |
| D | ASP60 |
| D | GLY61 |
| D | ASP91 |
| D | GLY92 |
| D | THR93 |
| D | THR94 |
| D | LYS161 |
| D | ASP386 |
| D | MG544 |
| D | ADP545 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG E 544 |
| Chain | Residue |
| E | ASP91 |
| E | SER157 |
| E | LYS161 |
| E | ASP386 |
| E | ADP545 |
| E | SO4546 |
| site_id | BC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ADP E 545 |
| Chain | Residue |
| E | THR38 |
| E | GLY40 |
| E | ASN59 |
| E | ASP91 |
| E | GLY92 |
| E | THR93 |
| E | THR94 |
| E | THR95 |
| E | GLY160 |
| E | GLY403 |
| E | GLY404 |
| E | LEU473 |
| E | PHE476 |
| E | GLU490 |
| E | MG544 |
| E | SO4546 |
| site_id | BC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 E 546 |
| Chain | Residue |
| E | ASP60 |
| E | GLY61 |
| E | ASP91 |
| E | GLY92 |
| E | THR93 |
| E | THR94 |
| E | LYS161 |
| E | ASP386 |
| E | MG544 |
| E | ADP545 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 544 |
| Chain | Residue |
| F | ASP91 |
| F | SER157 |
| F | LYS161 |
| F | ASP386 |
| F | ADP545 |
| F | SO4546 |
| site_id | BC8 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADP F 545 |
| Chain | Residue |
| F | THR38 |
| F | GLY40 |
| F | ASN59 |
| F | ASP91 |
| F | GLY92 |
| F | THR93 |
| F | THR94 |
| F | THR95 |
| F | GLY160 |
| F | GLY403 |
| F | GLY404 |
| F | LEU473 |
| F | GLU490 |
| F | MG544 |
| F | SO4546 |
| site_id | BC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 F 546 |
| Chain | Residue |
| F | ASP60 |
| F | GLY61 |
| F | ASP91 |
| F | GLY92 |
| F | THR93 |
| F | THR94 |
| F | LYS161 |
| F | ASP386 |
| F | MG544 |
| F | ADP545 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG G 544 |
| Chain | Residue |
| G | ASP91 |
| G | SER157 |
| G | ASP386 |
| G | ADP545 |
| G | SO4546 |
| site_id | CC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADP G 545 |
| Chain | Residue |
| G | THR38 |
| G | GLY40 |
| G | ASN59 |
| G | ASP91 |
| G | GLY92 |
| G | THR93 |
| G | THR94 |
| G | THR95 |
| G | GLY160 |
| G | GLY403 |
| G | GLY404 |
| G | LEU473 |
| G | GLU490 |
| G | MG544 |
| G | SO4546 |
| site_id | CC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 G 546 |
| Chain | Residue |
| G | ASP60 |
| G | GLY61 |
| G | ASP91 |
| G | GLY92 |
| G | THR93 |
| G | THR94 |
| G | LYS161 |
| G | ASP386 |
| G | MG544 |
| G | ADP545 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG H 544 |
| Chain | Residue |
| H | ASP91 |
| H | SER157 |
| H | ASP386 |
| H | ADP545 |
| H | SO4546 |
| site_id | CC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADP H 545 |
| Chain | Residue |
| H | THR38 |
| H | GLY40 |
| H | ASN59 |
| H | ASP91 |
| H | GLY92 |
| H | THR93 |
| H | THR94 |
| H | THR95 |
| H | GLY160 |
| H | GLY403 |
| H | GLY404 |
| H | LEU473 |
| H | GLU490 |
| H | MG544 |
| H | SO4546 |
| site_id | CC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SO4 H 546 |
| Chain | Residue |
| H | ASP60 |
| H | GLY61 |
| H | ASP91 |
| H | GLY92 |
| H | THR93 |
| H | THR94 |
| H | LYS161 |
| H | ASP386 |
| H | MG544 |
| H | ADP545 |
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 |
