5D4W
Crystal structure of Hsp104
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006457 | biological_process | protein folding |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0034605 | biological_process | cellular response to heat |
| A | 0042026 | biological_process | protein refolding |
| A | 0043335 | biological_process | protein unfolding |
| A | 0051087 | molecular_function | protein-folding chaperone binding |
| A | 0070370 | biological_process | cellular heat acclimation |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006457 | biological_process | protein folding |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0034605 | biological_process | cellular response to heat |
| B | 0042026 | biological_process | protein refolding |
| B | 0043335 | biological_process | protein unfolding |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
| B | 0070370 | biological_process | cellular heat acclimation |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006457 | biological_process | protein folding |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0034605 | biological_process | cellular response to heat |
| C | 0042026 | biological_process | protein refolding |
| C | 0043335 | biological_process | protein unfolding |
| C | 0051087 | molecular_function | protein-folding chaperone binding |
| C | 0070370 | biological_process | cellular heat acclimation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue ADP A 1001 |
| Chain | Residue |
| A | VAL197 |
| A | LYS229 |
| A | THR230 |
| A | THR231 |
| A | ILE367 |
| A | LEU371 |
| A | TYR375 |
| A | ASP406 |
| A | VAL409 |
| B | ARG349 |
| A | ILE198 |
| A | GLY199 |
| A | ARG200 |
| A | GLU224 |
| A | PRO225 |
| A | GLY226 |
| A | VAL227 |
| A | GLY228 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue ADP A 1002 |
| Chain | Residue |
| A | VAL600 |
| A | SER636 |
| A | THR638 |
| A | GLY639 |
| A | LYS640 |
| A | THR641 |
| A | LEU642 |
| A | ASP706 |
| A | ILE806 |
| B | ARG788 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | binding site for residue ADP B 1001 |
| Chain | Residue |
| B | VAL197 |
| B | ILE198 |
| B | GLY199 |
| B | ARG200 |
| B | GLU224 |
| B | PRO225 |
| B | GLY226 |
| B | VAL227 |
| B | GLY228 |
| B | LYS229 |
| B | THR230 |
| B | THR231 |
| B | ILE367 |
| B | LEU371 |
| B | TYR375 |
| B | ASP406 |
| B | VAL409 |
| C | ARG349 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | binding site for residue ADP B 1002 |
| Chain | Residue |
| B | VAL600 |
| B | VAL601 |
| B | THR638 |
| B | GLY639 |
| B | LYS640 |
| B | THR641 |
| B | LEU642 |
| B | ILE806 |
| B | ARG849 |
| C | ARG788 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue ADP C 1001 |
| Chain | Residue |
| C | VAL197 |
| C | ILE198 |
| C | GLY199 |
| C | ARG200 |
| C | GLU224 |
| C | PRO225 |
| C | GLY226 |
| C | VAL227 |
| C | GLY228 |
| C | LYS229 |
| C | THR230 |
| C | THR231 |
| C | ILE367 |
| C | LEU371 |
| C | TYR375 |
| C | PRO405 |
| C | ASP406 |
| C | VAL409 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue ADP C 1002 |
| Chain | Residue |
| C | VAL600 |
| C | VAL601 |
| C | THR638 |
| C | GLY639 |
| C | LYS640 |
| C | THR641 |
| C | LEU642 |
| C | ILE806 |
| C | ARG810 |
| C | ALA848 |
Functional Information from PROSITE/UniProt
