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 | |