Functional Information from GO Data
Chain | GOid | namespace | contents |
X | 0004176 | molecular_function | ATP-dependent peptidase activity |
X | 0005515 | molecular_function | protein binding |
X | 0005524 | molecular_function | ATP binding |
X | 0005737 | cellular_component | cytoplasm |
X | 0005829 | cellular_component | cytosol |
X | 0006508 | biological_process | proteolysis |
X | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
X | 0006979 | biological_process | response to oxidative stress |
X | 0009368 | cellular_component | endopeptidase Clp complex |
X | 0016887 | molecular_function | ATP hydrolysis activity |
X | 0034605 | biological_process | cellular response to heat |
X | 0043335 | biological_process | protein unfolding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG X 782 |
Chain | Residue |
X | LYS501 |
X | ADP781 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE MG X 783 |
Chain | Residue |
X | ASP520 |
X | SER522 |
X | GLU565 |
X | GLU639 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE PGE X 785 |
Chain | Residue |
X | VAL110 |
X | ALA111 |
X | ILE138 |
X | ASP674 |
X | HOH908 |
X | ARG90 |
X | HIS94 |
X | ASN107 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PGE X 786 |
Chain | Residue |
X | LYS387 |
X | TYR388 |
X | ALA434 |
X | ARG435 |
X | GLU484 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE ADP X 780 |
Chain | Residue |
X | PRO187 |
X | LEU188 |
X | ILE189 |
X | ARG206 |
X | GLU215 |
X | GLY217 |
X | GLY219 |
X | LYS220 |
X | THR221 |
X | ALA222 |
X | ARG339 |
X | ASP396 |
X | ILE399 |
X | HOH901 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE ADP X 781 |
Chain | Residue |
X | LEU459 |
X | VAL460 |
X | PHE461 |
X | GLN463 |
X | GLY498 |
X | VAL499 |
X | GLY500 |
X | LYS501 |
X | THR502 |
X | GLU503 |
X | LEU653 |
X | VAL661 |
X | PHE665 |
X | ALA701 |
X | MG782 |
X | HOH977 |
X | HOH982 |
X | HOH1073 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IPA X 791 |
Chain | Residue |
X | GLU523 |
X | THR637 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IPA X 792 |
Chain | Residue |
X | GLN89 |
X | PHE93 |
X | ASP663 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE IPA X 794 |
Chain | Residue |
X | SER97 |
X | ARG435 |
X | GLN672 |
X | GLN675 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IPA X 795 |
Chain | Residue |
X | GLU102 |
X | GLU427 |
X | HOH968 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE IPA X 796 |
Chain | Residue |
X | PRO349 |
X | LEU394 |
X | HOH891 |
Functional Information from PROSITE/UniProt
site_id | PS00870 |
Number of Residues | 13 |
Details | CLPAB_1 Chaperonins clpA/B signature 1. DAANLIKPlLssG |
Chain | Residue | Details |
X | ASP302-GLY314 | |
site_id | PS00871 |
Number of Residues | 19 |
Details | CLPAB_2 Chaperonins clpA/B signature 2. RFDmSEYmERhTvSRLiGA |
Chain | Residue | Details |
X | ARG518-ALA536 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
X | GLY214 | |
X | GLY495 | |