Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0009408 | biological_process | response to heat |
A | 0016020 | cellular_component | membrane |
A | 0016887 | molecular_function | ATP hydrolysis activity |
A | 0034605 | biological_process | cellular response to heat |
A | 0042026 | biological_process | protein refolding |
A | 0042802 | molecular_function | identical protein binding |
A | 0043335 | biological_process | protein unfolding |
F | 0000166 | molecular_function | nucleotide binding |
F | 0005515 | molecular_function | protein binding |
F | 0005524 | molecular_function | ATP binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0005829 | cellular_component | cytosol |
F | 0009408 | biological_process | response to heat |
F | 0016020 | cellular_component | membrane |
F | 0016887 | molecular_function | ATP hydrolysis activity |
F | 0034605 | biological_process | cellular response to heat |
F | 0042026 | biological_process | protein refolding |
F | 0042802 | molecular_function | identical protein binding |
F | 0043335 | biological_process | protein unfolding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | binding site for residue ADP F 901 |
Chain | Residue |
F | ASP178 |
F | PRO179 |
F | VAL180 |
F | ILE181 |
F | PRO208 |
F | GLY209 |
F | PRO387 |
F | ILE391 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue ADP F 902 |
Chain | Residue |
F | GLY608 |
F | THR612 |
F | GLU613 |
F | ILE774 |
F | GLN778 |
F | ARG815 |
F | GLN573 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue AGS A 901 |
Chain | Residue |
A | ASP178 |
A | PRO179 |
A | VAL180 |
A | ILE181 |
A | ARG183 |
A | PRO208 |
A | GLY209 |
A | VAL210 |
A | GLY211 |
A | LYS212 |
A | THR213 |
A | ALA214 |
A | ILE349 |
A | PRO387 |
A | ILE391 |
F | ARG331 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue ADP A 902 |
Chain | Residue |
A | ARG569 |
A | VAL570 |
A | ILE571 |
A | THR607 |
A | GLY608 |
A | VAL609 |
A | GLY610 |
A | THR612 |
A | GLU613 |
A | ILE774 |
A | ALA814 |
A | ARG815 |
A | LYS818 |
Functional Information from PROSITE/UniProt
site_id | PS00870 |
Number of Residues | 13 |
Details | CLPAB_1 Chaperonins clpA/B signature 1. DAGNMLKPaLarG |
Chain | Residue | Details |
F | ASP294-GLY306 | |
site_id | PS00871 |
Number of Residues | 19 |
Details | CLPAB_2 Chaperonins clpA/B signature 2. RIDmSEFmEKhSvSRLvGA |
Chain | Residue | Details |
F | ARG631-ALA649 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
F | GLY206 | |
F | GLY605 | |
A | GLY206 | |
A | GLY605 | |
Chain | Residue | Details |
F | ASN96 | |
F | LYS176 | |
F | LYS640 | |
A | ASN96 | |
A | LYS176 | |
A | LYS640 | |