5W74
Crystal Structure of the Group II Chaperonin from Methanococcus Maripaludis D386ADeltaLid Mutant in the Open, ADP-Bound State
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 | 0016787 | molecular_function | hydrolase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0032991 | cellular_component | protein-containing complex |
| 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 | 0016787 | molecular_function | hydrolase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0032991 | cellular_component | protein-containing complex |
| 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 | 0016787 | molecular_function | hydrolase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0032991 | cellular_component | protein-containing complex |
| 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 | 0016787 | molecular_function | hydrolase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0032991 | cellular_component | protein-containing complex |
| 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 | 0016787 | molecular_function | hydrolase activity |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0032991 | cellular_component | protein-containing complex |
| 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 | 0016787 | molecular_function | hydrolase activity |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0032991 | cellular_component | protein-containing complex |
| 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 | 0016787 | molecular_function | hydrolase activity |
| G | 0016853 | molecular_function | isomerase activity |
| G | 0016887 | molecular_function | ATP hydrolysis activity |
| G | 0032991 | cellular_component | protein-containing complex |
| 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 | 0016787 | molecular_function | hydrolase activity |
| H | 0016853 | molecular_function | isomerase activity |
| H | 0016887 | molecular_function | ATP hydrolysis activity |
| H | 0032991 | cellular_component | protein-containing complex |
| 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 | 16 |
| Details | binding site for residue ADP A 600 |
| Chain | Residue |
| A | LEU39 |
| A | GLY405 |
| A | LEU473 |
| A | ASN474 |
| A | VAL488 |
| A | GLU490 |
| A | LYS495 |
| A | MG601 |
| A | GLY40 |
| A | ASP91 |
| A | GLY92 |
| A | THR94 |
| A | THR95 |
| A | GLY160 |
| A | GLY403 |
| A | GLY404 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue MG A 601 |
| Chain | Residue |
| A | THR94 |
| A | ADP600 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | binding site for residue ADP B 600 |
| Chain | Residue |
| B | LEU39 |
| B | ASP91 |
| B | GLY92 |
| B | THR93 |
| B | THR94 |
| B | THR95 |
| B | THR156 |
| B | GLY160 |
| B | GLY403 |
| B | GLY404 |
| B | VAL488 |
| B | GLU490 |
| B | LYS495 |
| B | MG601 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | binding site for residue MG B 601 |
| Chain | Residue |
| B | ASP91 |
| B | ADP600 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | binding site for residue ADP C 600 |
| Chain | Residue |
| C | THR38 |
| C | LEU39 |
| C | GLY40 |
| C | PRO41 |
| C | ASP91 |
| C | GLY92 |
| C | THR93 |
| C | THR94 |
| C | THR95 |
| C | THR156 |
| C | THR159 |
| C | GLY160 |
| C | GLY404 |
| C | LEU473 |
| C | PHE476 |
| C | GLU490 |
| C | MG601 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue MG C 601 |
| Chain | Residue |
| C | ASP91 |
| C | SER157 |
| C | ADP600 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue ADP D 600 |
| Chain | Residue |
| D | LEU39 |
| D | GLY40 |
| D | PRO41 |
| D | ASP91 |
| D | GLY92 |
| D | THR93 |
| D | THR94 |
| D | THR95 |
| D | THR156 |
| D | GLY160 |
| D | GLY404 |
| D | GLU490 |
| D | LYS495 |
| D | MG601 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue MG D 601 |
| Chain | Residue |
| D | ASP91 |
| D | SER157 |
| D | ADP600 |
| site_id | AC9 |
| Number of Residues | 15 |
| Details | binding site for residue ADP E 600 |
| Chain | Residue |
| E | LEU39 |
| E | GLY40 |
| E | PRO41 |
| E | ASP91 |
| E | GLY92 |
| E | THR94 |
| E | THR95 |
| E | GLY160 |
| E | GLY403 |
| E | GLY404 |
| E | GLY405 |
| E | LEU473 |
| E | GLU490 |
| E | LYS495 |
| E | MG601 |
| site_id | AD1 |
| Number of Residues | 2 |
| Details | binding site for residue MG E 601 |
| Chain | Residue |
| E | ASP91 |
| E | ADP600 |
| site_id | AD2 |
| Number of Residues | 17 |
| Details | binding site for residue ADP F 600 |
| Chain | Residue |
| F | GLY404 |
| F | LEU473 |
| F | PHE476 |
| F | GLU490 |
| F | LYS495 |
| F | MG601 |
| F | THR38 |
| F | LEU39 |
| F | GLY40 |
| F | PRO41 |
| F | ASP91 |
| F | GLY92 |
| F | THR94 |
| F | THR95 |
| F | THR156 |
| F | GLY160 |
| F | GLY403 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue MG F 601 |
| Chain | Residue |
| F | ASP91 |
| F | SER157 |
| F | ADP600 |
| site_id | AD4 |
| Number of Residues | 15 |
| Details | binding site for residue ADP G 600 |
| Chain | Residue |
| G | LEU39 |
| G | GLY40 |
| G | PRO41 |
| G | ASP91 |
| G | GLY92 |
| G | THR94 |
| G | THR95 |
| G | GLY160 |
| G | GLY403 |
| G | GLY404 |
| G | LEU473 |
| G | VAL488 |
| G | GLU490 |
| G | LYS495 |
| G | MG601 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue MG G 601 |
| Chain | Residue |
| G | ASP91 |
| G | ADP600 |
| site_id | AD6 |
| Number of Residues | 18 |
| Details | binding site for residue ADP H 600 |
| Chain | Residue |
| H | THR38 |
| H | LEU39 |
| H | GLY40 |
| H | PRO41 |
| H | ASP91 |
| H | GLY92 |
| H | THR93 |
| H | THR94 |
| H | THR95 |
| H | THR156 |
| H | THR159 |
| H | GLY160 |
| H | GLY404 |
| H | PHE476 |
| H | VAL488 |
| H | GLU490 |
| H | LYS495 |
| H | MG601 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue MG H 601 |
| Chain | Residue |
| H | ASP91 |
| H | SER157 |
| H | ADP600 |
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 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 72 |
| Details | Region: {"description":"Nucleotide-sensing loop","evidences":[{"source":"PubMed","id":"22193720","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"20573955","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5W74","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5W74","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20573955","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUQ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20573955","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KFK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5W74","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20573955","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5W74","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22193720","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22193720","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3KFB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3RUS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Site: {"description":"ATP sensor","evidences":[{"source":"PubMed","id":"22193720","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |






