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 | 12 |
Details | binding site for residue AGS A 1001 |
Chain | Residue |
A | ASP178 |
A | ILE349 |
A | LEU353 |
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 | 17 |
Details | binding site for residue AGS B 1001 |
Chain | Residue |
A | ARG331 |
A | ARG332 |
B | ASP178 |
B | PRO179 |
B | VAL180 |
B | ILE181 |
B | PRO208 |
B | GLY209 |
B | GLY211 |
B | LYS212 |
B | THR213 |
B | ALA214 |
B | THR315 |
B | ILE349 |
B | LEU353 |
B | PRO387 |
B | ILE391 |
site_id | AC4 |
Number of Residues | 16 |
Details | binding site for residue AGS B 1002 |
Chain | Residue |
A | ARG756 |
B | ARG569 |
B | VAL570 |
B | ILE571 |
B | GLY572 |
B | THR607 |
B | GLY608 |
B | VAL609 |
B | GLY610 |
B | LYS611 |
B | THR612 |
B | GLU613 |
B | ASP677 |
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 | PRO208 |
C | GLY209 |
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 E 1001 |
Chain | Residue |
D | ARG331 |
D | ARG332 |
E | PRO179 |
E | VAL180 |
E | ILE181 |
E | GLY209 |
E | VAL210 |
E | GLY211 |
E | LYS212 |
E | THR213 |
E | ALA214 |
E | LEU353 |
E | PRO387 |
site_id | AC7 |
Number of Residues | 16 |
Details | binding site for Di-peptide AGS C 1002 and ILE C 571 |
Chain | Residue |
C | GLN778 |
C | ALA814 |
C | ARG815 |
B | ARG756 |
C | ARG569 |
C | VAL570 |
C | GLY572 |
C | GLY608 |
C | VAL609 |
C | GLY610 |
C | LYS611 |
C | THR612 |
C | GLU613 |
C | ASN719 |
C | SER773 |
C | ILE774 |
site_id | AC8 |
Number of Residues | 13 |
Details | binding site for Di-peptide AGS D 1001 and GLY D 211 |
Chain | Residue |
C | ARG331 |
C | ARG332 |
D | ILE181 |
D | ARG183 |
D | PRO208 |
D | GLY209 |
D | VAL210 |
D | LYS212 |
D | THR213 |
D | ALA214 |
D | ILE215 |
D | ILE349 |
D | PRO387 |
site_id | AC9 |
Number of Residues | 36 |
Details | binding site for Di-peptide AGS D 1001 and ARG C 332 |
Chain | Residue |
B | ARG331 |
B | ARG332 |
C | PRO179 |
C | VAL180 |
C | ILE181 |
C | ASN201 |
C | PRO208 |
C | GLY209 |
C | GLY211 |
C | LYS212 |
C | THR213 |
C | ALA214 |
C | LYS300 |
C | ALA328 |
C | GLU330 |
C | ARG331 |
C | PHE333 |
C | ILE349 |
C | LEU353 |
C | PRO387 |
D | ILE181 |
D | ARG183 |
D | PRO208 |
D | GLY209 |
D | VAL210 |
D | GLY211 |
D | LYS212 |
D | THR213 |
D | LEU303 |
D | LEU329 |
D | GLU330 |
D | ARG331 |
D | PHE333 |
D | ILE349 |
D | PRO387 |
E | AGS1001 |
site_id | AD1 |
Number of Residues | 16 |
Details | binding site for Di-peptide AGS D 1002 and THR D 607 |
Chain | Residue |
C | ASN755 |
C | ARG756 |
D | ILE571 |
D | PRO606 |
D | GLY608 |
D | VAL609 |
D | GLY610 |
D | LYS611 |
D | THR612 |
D | GLU613 |
D | ASN719 |
D | GLN778 |
D | GLY813 |
D | ALA814 |
D | ARG815 |
D | LYS818 |
site_id | AD2 |
Number of Residues | 16 |
Details | binding site for Di-peptide AGS D 1002 and THR D 607 |
Chain | Residue |
C | ASN755 |
C | ARG756 |
D | ILE571 |
D | PRO606 |
D | GLY608 |
D | VAL609 |
D | GLY610 |
D | LYS611 |
D | THR612 |
D | GLU613 |
D | ASN719 |
D | GLN778 |
D | GLY813 |
D | ALA814 |
D | ARG815 |
D | LYS818 |
site_id | AD3 |
Number of Residues | 19 |
Details | binding site for Di-peptide AGS E 1002 and VAL E 609 |
Chain | Residue |
D | ARG756 |
E | ARG569 |
E | VAL570 |
E | ILE571 |
E | GLY572 |
E | PRO606 |
E | THR607 |
E | GLY608 |
E | GLY610 |
E | LYS611 |
E | THR612 |
E | GLU613 |
E | PHE763 |
E | LEU766 |
E | ILE774 |
E | GLN778 |
E | ALA814 |
E | ARG815 |
E | LYS818 |
site_id | AD4 |
Number of Residues | 24 |
Details | binding site for Di-peptide AGS E 1002 and LYS E 611 |
Chain | Residue |
D | ARG756 |
E | ARG569 |
E | VAL570 |
E | ILE571 |
E | GLY572 |
E | LEU604 |
E | GLY605 |
E | PRO606 |
E | GLY608 |
E | VAL609 |
E | GLY610 |
E | THR612 |
E | GLU613 |
E | LEU614 |
E | CYS615 |
E | SER718 |
E | ASN719 |
E | PHE763 |
E | LEU766 |
E | ILE774 |
E | GLN778 |
E | ALA814 |
E | ARG815 |
E | LYS818 |
site_id | AD5 |
Number of Residues | 18 |
Details | binding site for Di-peptide AGS E 1002 and ILE E 571 |
Chain | Residue |
D | ARG756 |
E | HIS567 |
E | ARG569 |
E | VAL570 |
E | GLY572 |
E | GLY608 |
E | VAL609 |
E | GLY610 |
E | LYS611 |
E | THR612 |
E | GLU613 |
E | LEU766 |
E | SER773 |
E | ILE774 |
E | GLN778 |
E | ALA814 |
E | ARG815 |
E | LYS818 |
site_id | AD6 |
Number of Residues | 11 |
Details | binding site for Di-peptide ADP F 1001 and GLY F 211 |
Chain | Residue |
F | VAL180 |
F | ILE181 |
F | PRO208 |
F | GLY209 |
F | VAL210 |
F | LYS212 |
F | THR213 |
F | ALA214 |
F | ILE215 |
F | ILE349 |
F | ILE391 |
site_id | AD7 |
Number of Residues | 13 |
Details | binding site for Di-peptide ADP F 1001 and LYS F 212 |
Chain | Residue |
F | VAL180 |
F | ILE181 |
F | LEU204 |
F | PRO208 |
F | GLY209 |
F | VAL210 |
F | GLY211 |
F | THR213 |
F | ALA214 |
F | ILE215 |
F | VAL216 |
F | ILE349 |
F | ILE391 |
site_id | AD8 |
Number of Residues | 18 |
Details | binding site for Di-peptide ADP F 1001 and ILE F 349 |
Chain | Residue |
F | VAL180 |
F | ILE181 |
F | PRO208 |
F | GLY209 |
F | VAL210 |
F | GLY211 |
F | LYS212 |
F | THR213 |
F | ALA214 |
F | ASP345 |
F | THR346 |
F | ILE347 |
F | ALA348 |
F | LEU350 |
F | ARG351 |
F | GLY352 |
F | LEU353 |
F | ILE391 |
site_id | AD9 |
Number of Residues | 11 |
Details | binding site for Di-peptide ADP F 1001 and GLY F 209 |
Chain | Residue |
F | VAL180 |
F | ILE181 |
F | PRO208 |
F | VAL210 |
F | GLY211 |
F | LYS212 |
F | THR213 |
F | ALA214 |
F | ILE349 |
F | ASP388 |
F | 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 |
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 | |