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 A 1001 |
| Chain | Residue |
| A | ASP178 |
| A | ILE349 |
| A | LEU353 |
| A | ASP388 |
| A | ILE391 |
| F | ARG331 |
| A | VAL180 |
| A | ILE181 |
| A | PRO208 |
| A | GLY209 |
| A | VAL210 |
| A | GLY211 |
| A | LYS212 |
| A | THR213 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue ADP A 1002 |
| Chain | Residue |
| A | ARG569 |
| A | VAL570 |
| A | ILE571 |
| A | THR607 |
| A | GLY608 |
| A | VAL609 |
| A | GLY610 |
| A | LYS611 |
| A | THR612 |
| A | GLU613 |
| A | ILE774 |
| A | ALA814 |
| A | ARG815 |
| A | LYS818 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue AGS B 1001 |
| Chain | Residue |
| A | ARG331 |
| A | ARG332 |
| B | PRO179 |
| B | ILE181 |
| B | ARG183 |
| B | PRO208 |
| B | GLY209 |
| B | VAL210 |
| B | GLY211 |
| B | LYS212 |
| B | THR213 |
| B | ALA214 |
| B | ILE349 |
| B | LEU353 |
| B | ILE391 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue AGS B 1002 |
| Chain | Residue |
| A | ASP695 |
| A | ARG756 |
| B | ARG569 |
| B | VAL570 |
| B | ILE571 |
| B | GLY572 |
| B | PRO606 |
| B | THR607 |
| B | GLY608 |
| B | VAL609 |
| B | GLY610 |
| B | LYS611 |
| B | THR612 |
| B | GLU613 |
| B | ASN719 |
| B | LEU766 |
| B | ILE774 |
| B | ALA814 |
| B | ARG815 |
| B | LYS818 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | binding site for residue AGS C 1001 |
| Chain | Residue |
| B | ARG331 |
| B | ARG332 |
| C | PRO179 |
| C | VAL180 |
| C | ILE181 |
| C | GLY209 |
| C | VAL210 |
| C | GLY211 |
| C | LYS212 |
| C | THR213 |
| C | ALA214 |
| C | ILE349 |
| C | LEU353 |
| C | PRO387 |
| site_id | AC6 |
| Number of Residues | 13 |
| Details | binding site for residue AGS C 1002 |
| Chain | Residue |
| B | ARG756 |
| C | ARG569 |
| C | VAL570 |
| C | ILE571 |
| C | GLY608 |
| C | VAL609 |
| C | GLY610 |
| C | LYS611 |
| C | THR612 |
| C | GLU613 |
| C | ILE774 |
| C | ARG815 |
| C | LYS818 |
| site_id | AC7 |
| Number of Residues | 41 |
| Details | binding site for Di-peptide AGS D 1001 and ARG C 332 |
| Chain | Residue |
| C | LYS212 |
| C | THR213 |
| C | ALA214 |
| C | LYS300 |
| C | ALA304 |
| C | ALA328 |
| C | GLU330 |
| C | ARG331 |
| C | PHE333 |
| C | ILE349 |
| C | LEU353 |
| C | PRO387 |
| D | PRO179 |
| D | VAL180 |
| D | ILE181 |
| D | ASN201 |
| D | PRO208 |
| D | GLY209 |
| D | VAL210 |
| D | GLY211 |
| D | LYS212 |
| D | THR213 |
| D | LEU303 |
| D | ALA328 |
| D | LEU329 |
| D | GLU330 |
| D | ARG331 |
| D | PHE333 |
| D | ILE349 |
| D | LEU353 |
| D | PRO387 |
| D | ILE391 |
| B | ARG331 |
| B | ARG332 |
| C | PRO179 |
| C | VAL180 |
| C | ILE181 |
| C | LYS199 |
| C | GLY209 |
| C | VAL210 |
| C | GLY211 |
| site_id | AC8 |
| Number of Residues | 17 |
| Details | binding site for Di-peptide AGS D 1001 and GLY D 211 |
| Chain | Residue |
| C | ALA304 |
| C | ARG331 |
| C | ARG332 |
| D | PRO179 |
| D | VAL180 |
| D | ILE181 |
| D | PRO208 |
| D | GLY209 |
| D | VAL210 |
| D | LYS212 |
| D | THR213 |
| D | ALA214 |
| D | ILE215 |
| D | ILE349 |
| D | LEU353 |
| D | PRO387 |
| D | ILE391 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | binding site for Di-peptide AGS D 1001 and GLY D 211 |
| Chain | Residue |
| C | ALA304 |
| C | ARG331 |
| C | ARG332 |
| D | PRO179 |
| D | VAL180 |
| D | ILE181 |
| D | PRO208 |
| D | GLY209 |
| D | VAL210 |
| D | LYS212 |
| D | THR213 |
| D | ALA214 |
| D | ILE215 |
| D | ILE349 |
| D | LEU353 |
| D | PRO387 |
| D | ILE391 |
| site_id | AD1 |
| Number of Residues | 17 |
| Details | binding site for Di-peptide AGS D 1002 and THR D 607 |
| Chain | Residue |
| C | ASP695 |
| C | ARG756 |
| D | ARG569 |
| D | VAL570 |
| D | ILE571 |
| D | GLY605 |
| D | PRO606 |
| D | GLY608 |
| D | VAL609 |
| D | GLY610 |
| D | LYS611 |
| D | THR612 |
| D | GLU613 |
| D | TYR812 |
| D | ALA814 |
| D | ARG815 |
| D | LYS818 |
| site_id | AD2 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide AGS E 1001 and ALA E 214 |
| Chain | Residue |
| D | ARG331 |
| E | VAL180 |
| E | PRO208 |
| E | GLY209 |
| E | GLY211 |
| E | LYS212 |
| E | THR213 |
| E | ILE215 |
| E | VAL216 |
| E | GLU217 |
| E | GLY218 |
| E | ILE349 |
| E | PRO387 |
| E | ASP388 |
| E | ILE391 |
| site_id | AD3 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide AGS E 1001 and ALA E 214 |
| Chain | Residue |
| D | ARG331 |
| E | VAL180 |
| E | PRO208 |
| E | GLY209 |
| E | GLY211 |
| E | LYS212 |
| E | THR213 |
| E | ILE215 |
| E | VAL216 |
| E | GLU217 |
| E | GLY218 |
| E | ILE349 |
| E | PRO387 |
| E | ASP388 |
| E | ILE391 |
| site_id | AD4 |
| Number of Residues | 15 |
| Details | binding site for Di-peptide AGS E 1001 and VAL E 180 |
| Chain | Residue |
| D | ARG331 |
| E | ASP178 |
| E | PRO179 |
| E | ILE181 |
| E | GLY182 |
| E | PRO208 |
| E | GLY209 |
| E | GLY211 |
| E | LYS212 |
| E | THR213 |
| E | ALA214 |
| E | ILE349 |
| E | PRO387 |
| E | ASP388 |
| E | ILE391 |
| site_id | AD5 |
| Number of Residues | 23 |
| Details | binding site for Di-peptide AGS E 1002 and ARG E 569 |
| Chain | Residue |
| D | ARG756 |
| E | GLU565 |
| E | LEU566 |
| E | HIS567 |
| E | HIS568 |
| E | VAL570 |
| E | ILE571 |
| E | THR607 |
| E | GLY608 |
| E | VAL609 |
| E | GLY610 |
| E | LYS611 |
| E | THR612 |
| E | GLU613 |
| E | LYS616 |
| E | ALA617 |
| E | ASN620 |
| E | ASP677 |
| E | LEU766 |
| E | ILE774 |
| E | ALA814 |
| E | ARG815 |
| E | LYS818 |
| site_id | AD6 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide AGS E 1002 and THR E 612 |
| Chain | Residue |
| D | ARG756 |
| E | ARG569 |
| E | VAL570 |
| E | ILE571 |
| E | THR607 |
| E | GLY608 |
| E | VAL609 |
| E | GLY610 |
| E | LYS611 |
| E | GLU613 |
| E | LEU614 |
| E | CYS615 |
| E | LYS616 |
| E | ARG631 |
| E | ASP677 |
| E | LEU766 |
| E | ILE774 |
| E | ALA814 |
| E | ARG815 |
| E | LYS818 |
| site_id | AD7 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide AGS E 1002 and GLU E 613 |
| Chain | Residue |
| D | ARG756 |
| E | ARG569 |
| E | VAL570 |
| E | ILE571 |
| E | THR607 |
| E | GLY608 |
| E | VAL609 |
| E | GLY610 |
| E | LYS611 |
| E | THR612 |
| E | LEU614 |
| E | CYS615 |
| E | LYS616 |
| E | ALA617 |
| E | ASP677 |
| E | LEU766 |
| E | ILE774 |
| E | ALA814 |
| E | ARG815 |
| E | LYS818 |
| site_id | AD8 |
| Number of Residues | 21 |
| Details | binding site for Di-peptide ADP E 1003 and ASP F 178 |
| Chain | Residue |
| E | LEU177 |
| E | PRO179 |
| E | VAL180 |
| E | GLN221 |
| E | ARG331 |
| E | ARG356 |
| F | LEU177 |
| F | PRO179 |
| F | VAL180 |
| F | ILE181 |
| F | PRO208 |
| F | GLY209 |
| F | VAL210 |
| F | GLY211 |
| F | LYS212 |
| F | THR213 |
| F | ALA214 |
| F | GLU217 |
| F | GLN221 |
| F | ILE349 |
| F | PRO387 |
| site_id | AD9 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide ADP E 1003 and VAL F 180 |
| Chain | Residue |
| E | ASP178 |
| E | PRO179 |
| E | ILE181 |
| E | GLY182 |
| E | ALA214 |
| E | ARG331 |
| E | AGS1001 |
| F | ASP178 |
| F | PRO179 |
| F | ILE181 |
| F | PRO208 |
| F | GLY209 |
| F | VAL210 |
| F | GLY211 |
| F | LYS212 |
| F | THR213 |
| F | ALA214 |
| F | GLU217 |
| F | ILE349 |
| F | PRO387 |
| site_id | AE1 |
| Number of Residues | 23 |
| Details | binding site for Di-peptide ADP E 1003 and THR F 213 |
| Chain | Residue |
| E | GLY211 |
| E | LYS212 |
| E | ALA214 |
| E | ILE215 |
| E | VAL216 |
| E | GLU217 |
| E | ARG331 |
| E | AGS1001 |
| F | ASP178 |
| F | PRO179 |
| F | VAL180 |
| F | ILE181 |
| F | PRO208 |
| F | GLY209 |
| F | VAL210 |
| F | GLY211 |
| F | LYS212 |
| F | ALA214 |
| F | ILE215 |
| F | VAL216 |
| F | GLU217 |
| F | ILE349 |
| F | PRO387 |
| site_id | AE2 |
| Number of Residues | 20 |
| Details | binding site for Di-peptide ADP E 1003 and ARG E 331 |
| Chain | Residue |
| E | LYS199 |
| E | ALA327 |
| E | LEU329 |
| E | GLU330 |
| E | ARG332 |
| E | PHE333 |
| F | ASP178 |
| F | PRO179 |
| F | VAL180 |
| F | ILE181 |
| F | PRO208 |
| F | GLY209 |
| F | VAL210 |
| F | GLY211 |
| F | LYS212 |
| F | THR213 |
| F | ALA214 |
| F | GLU217 |
| F | ILE349 |
| F | PRO387 |
Functional Information from PROSITE/UniProt
| site_id | PS00870 |
| Number of Residues | 13 |
| Details | CLPAB_1 Chaperonins clpA/B signature 1. DAGNMLKPaLarG |
| Chain | Residue | Details |
| A | ASP294-GLY306 | |
| site_id | PS00871 |
| Number of Residues | 19 |
| Details | CLPAB_2 Chaperonins clpA/B signature 2. RIDmSEFmEKhSvSRLvGA |
| Chain | Residue | Details |
| A | ARG631-ALA649 | |