Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0009408 | biological_process | response to heat |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0042026 | biological_process | protein refolding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0009408 | biological_process | response to heat |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0042026 | biological_process | protein refolding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0009408 | biological_process | response to heat |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0042026 | biological_process | protein refolding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0009408 | biological_process | response to heat |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0042026 | biological_process | protein refolding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0009408 | biological_process | response to heat |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0042026 | biological_process | protein refolding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0009408 | biological_process | response to heat |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0042026 | biological_process | protein refolding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue AGS C 901 |
| Chain | Residue |
| B | ARG332 |
| C | THR315 |
| C | ILE349 |
| C | LEU353 |
| C | TYR357 |
| C | ILE391 |
| C | ASP178 |
| C | PRO179 |
| C | VAL180 |
| C | GLY209 |
| C | GLY211 |
| C | LYS212 |
| C | THR213 |
| C | ALA214 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue AGS C 902 |
| Chain | Residue |
| B | ASP593 |
| B | LEU691 |
| B | ASP695 |
| B | ASP696 |
| B | GLU752 |
| B | ARG756 |
| C | GLY610 |
| C | LYS611 |
| C | THR612 |
| C | GLU613 |
| C | ARG631 |
| C | ARG815 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | binding site for residue AGS E 901 |
| Chain | Residue |
| E | ARG183 |
| E | GLY209 |
| E | VAL210 |
| E | GLY211 |
| E | LYS212 |
| E | THR213 |
| E | ALA214 |
| E | ASP278 |
| E | ALA313 |
| E | ILE349 |
| E | PRO387 |
| E | ASP388 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | binding site for residue AGS E 902 |
| Chain | Residue |
| D | ASP696 |
| E | ARG569 |
| E | GLY610 |
| E | LYS611 |
| E | THR612 |
| E | GLU613 |
| E | ARG631 |
| E | ASP677 |
| E | THR717 |
| E | ASN719 |
| E | GLN778 |
| E | ARG815 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | binding site for residue AGS D 901 |
| Chain | Residue |
| C | ALA328 |
| D | PRO208 |
| D | GLY209 |
| D | VAL210 |
| D | GLY211 |
| D | LYS212 |
| D | THR213 |
| D | PRO387 |
| D | ASP388 |
| D | ILE391 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | binding site for residue AGS D 902 |
| Chain | Residue |
| C | LEU691 |
| C | ASP695 |
| C | ARG750 |
| C | GLU752 |
| D | VAL609 |
| D | GLY610 |
| D | LYS611 |
| D | THR612 |
| D | GLU613 |
| D | LYS616 |
| D | ARG631 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue AGS B 901 |
| Chain | Residue |
| A | ALA327 |
| A | ARG331 |
| B | PRO179 |
| B | ARG183 |
| B | GLU207 |
| B | PRO208 |
| B | VAL210 |
| B | GLY211 |
| B | THR213 |
| B | ALA214 |
| B | LEU353 |
| B | TYR357 |
| B | ASP388 |
| B | ILE391 |
Functional Information from PROSITE/UniProt
| site_id | PS00870 |
| Number of Residues | 13 |
| Details | CLPAB_1 Chaperonins clpA/B signature 1. DAGNMLKPaLarG |
| Chain | Residue | Details |
| C | ASP294-GLY306 | |
| site_id | PS00871 |
| Number of Residues | 19 |
| Details | CLPAB_2 Chaperonins clpA/B signature 2. RIDmSEFmEKhSvSRLvGA |
| Chain | Residue | Details |
| C | ARG631-ALA649 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 84 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1260 |
| Details | Region: {"description":"NBD2"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 546 |
| Details | Region: {"description":"C-terminal"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 13 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 612 |
| Details | Region: {"description":"Linker"} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 402 |
| Details | Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 65 |
| Details | Region: {"description":"Repeat 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01251","evidenceCode":"ECO:0000255"}]} |