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 C 901 |
Chain | Residue |
B | ARG332 |
C | ALA214 |
C | ILE349 |
C | PRO387 |
C | VAL180 |
C | GLU207 |
C | PRO208 |
C | GLY209 |
C | VAL210 |
C | GLY211 |
C | LYS212 |
C | THR213 |
site_id | AC2 |
Number of Residues | 12 |
Details | binding site for residue AGS C 902 |
Chain | Residue |
B | GLU752 |
B | ARG756 |
C | ARG569 |
C | ILE571 |
C | GLY608 |
C | VAL609 |
C | GLY610 |
C | LYS611 |
C | THR612 |
C | GLU613 |
C | ALA814 |
C | ARG815 |
site_id | AC3 |
Number of Residues | 17 |
Details | binding site for residue AGS F 901 |
Chain | Residue |
E | ALA327 |
E | GLU330 |
E | ARG331 |
F | PRO179 |
F | VAL180 |
F | ILE181 |
F | ARG183 |
F | GLU207 |
F | PRO208 |
F | GLY209 |
F | VAL210 |
F | GLY211 |
F | LYS212 |
F | THR213 |
F | ALA214 |
F | ILE349 |
F | PRO387 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue AGS F 902 |
Chain | Residue |
F | THR607 |
F | GLY608 |
F | VAL609 |
F | GLY610 |
F | LYS611 |
F | THR612 |
F | GLU613 |
F | ARG631 |
F | LEU766 |
F | ILE774 |
F | ARG815 |
site_id | AC5 |
Number of Residues | 11 |
Details | binding site for residue AGS E 901 |
Chain | Residue |
D | ARG331 |
E | ILE181 |
E | GLY209 |
E | VAL210 |
E | GLY211 |
E | LYS212 |
E | THR213 |
E | ALA214 |
E | ASP278 |
E | ILE349 |
E | LEU353 |
site_id | AC6 |
Number of Residues | 11 |
Details | binding site for residue AGS E 902 |
Chain | Residue |
D | GLU752 |
E | ARG569 |
E | THR607 |
E | GLY608 |
E | VAL609 |
E | GLY610 |
E | LYS611 |
E | THR612 |
E | GLU613 |
E | ASN719 |
E | ARG815 |
site_id | AC7 |
Number of Residues | 14 |
Details | binding site for residue AGS D 901 |
Chain | Residue |
C | ARG331 |
C | ARG332 |
D | PRO179 |
D | ARG183 |
D | GLU207 |
D | GLY209 |
D | VAL210 |
D | GLY211 |
D | LYS212 |
D | THR213 |
D | ALA214 |
D | ILE349 |
D | PRO387 |
D | ASP388 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue AGS D 902 |
Chain | Residue |
D | ILE774 |
C | ASP695 |
C | ARG750 |
C | GLU752 |
D | ILE571 |
D | THR607 |
D | GLY608 |
D | VAL609 |
D | GLY610 |
D | LYS611 |
D | THR612 |
D | GLU613 |
site_id | AC9 |
Number of Residues | 12 |
Details | binding site for residue AGS B 901 |
Chain | Residue |
A | ARG331 |
A | ARG332 |
B | VAL180 |
B | GLU207 |
B | PRO208 |
B | VAL210 |
B | GLY211 |
B | LYS212 |
B | THR213 |
B | ALA214 |
B | ILE349 |
B | PRO387 |
site_id | AD1 |
Number of Residues | 11 |
Details | binding site for residue AGS B 902 |
Chain | Residue |
B | ARG569 |
B | GLY608 |
B | VAL609 |
B | GLY610 |
B | LYS611 |
B | THR612 |
B | GLU613 |
B | ASN719 |
B | ILE774 |
B | ALA814 |
B | ARG815 |
site_id | AD2 |
Number of Residues | 14 |
Details | binding site for residue AGS A 901 |
Chain | Residue |
A | ASP178 |
A | VAL180 |
A | ILE181 |
A | ARG183 |
A | GLY209 |
A | VAL210 |
A | GLY211 |
A | LYS212 |
A | THR213 |
A | ALA214 |
A | ILE349 |
A | LEU353 |
A | PRO387 |
F | ARG331 |
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 | 12 |
Details | BINDING: |
Chain | Residue | Details |
C | GLY206 | |
B | GLY605 | |
A | GLY206 | |
A | GLY605 | |
C | GLY605 | |
F | GLY206 | |
F | GLY605 | |
E | GLY206 | |
E | GLY605 | |
D | GLY206 | |
D | GLY605 | |
B | GLY206 | |
Chain | Residue | Details |
C | LYS96 | |
D | LYS96 | |
D | LYS176 | |
D | LYS640 | |
B | LYS96 | |
B | LYS176 | |
B | LYS640 | |
A | LYS96 | |
A | LYS176 | |
A | LYS640 | |
C | LYS176 | |
C | LYS640 | |
F | LYS96 | |
F | LYS176 | |
F | LYS640 | |
E | LYS96 | |
E | LYS176 | |
E | LYS640 | |