6N8Z
HSP104DWB extended conformation
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 | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005991 | biological_process | trehalose metabolic process |
| A | 0006457 | biological_process | protein folding |
| A | 0006620 | biological_process | post-translational protein targeting to endoplasmic reticulum membrane |
| A | 0016887 | molecular_function | ATP hydrolysis activity |
| A | 0034399 | cellular_component | nuclear periphery |
| A | 0034605 | biological_process | cellular response to heat |
| A | 0034975 | biological_process | protein folding in endoplasmic reticulum |
| A | 0035617 | biological_process | stress granule disassembly |
| A | 0042026 | biological_process | protein refolding |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043335 | biological_process | protein unfolding |
| A | 0043531 | molecular_function | ADP binding |
| A | 0051082 | molecular_function | unfolded protein binding |
| A | 0051087 | molecular_function | protein-folding chaperone binding |
| A | 0070013 | cellular_component | intracellular organelle lumen |
| A | 0070370 | biological_process | cellular heat acclimation |
| A | 0072380 | cellular_component | TRC complex |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005991 | biological_process | trehalose metabolic process |
| B | 0006457 | biological_process | protein folding |
| B | 0006620 | biological_process | post-translational protein targeting to endoplasmic reticulum membrane |
| B | 0016887 | molecular_function | ATP hydrolysis activity |
| B | 0034399 | cellular_component | nuclear periphery |
| B | 0034605 | biological_process | cellular response to heat |
| B | 0034975 | biological_process | protein folding in endoplasmic reticulum |
| B | 0035617 | biological_process | stress granule disassembly |
| B | 0042026 | biological_process | protein refolding |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043335 | biological_process | protein unfolding |
| B | 0043531 | molecular_function | ADP binding |
| B | 0051082 | molecular_function | unfolded protein binding |
| B | 0051087 | molecular_function | protein-folding chaperone binding |
| B | 0070013 | cellular_component | intracellular organelle lumen |
| B | 0070370 | biological_process | cellular heat acclimation |
| B | 0072380 | cellular_component | TRC complex |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005991 | biological_process | trehalose metabolic process |
| C | 0006457 | biological_process | protein folding |
| C | 0006620 | biological_process | post-translational protein targeting to endoplasmic reticulum membrane |
| C | 0016887 | molecular_function | ATP hydrolysis activity |
| C | 0034399 | cellular_component | nuclear periphery |
| C | 0034605 | biological_process | cellular response to heat |
| C | 0034975 | biological_process | protein folding in endoplasmic reticulum |
| C | 0035617 | biological_process | stress granule disassembly |
| C | 0042026 | biological_process | protein refolding |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0043335 | biological_process | protein unfolding |
| C | 0043531 | molecular_function | ADP binding |
| C | 0051082 | molecular_function | unfolded protein binding |
| C | 0051087 | molecular_function | protein-folding chaperone binding |
| C | 0070013 | cellular_component | intracellular organelle lumen |
| C | 0070370 | biological_process | cellular heat acclimation |
| C | 0072380 | cellular_component | TRC complex |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0005991 | biological_process | trehalose metabolic process |
| D | 0006457 | biological_process | protein folding |
| D | 0006620 | biological_process | post-translational protein targeting to endoplasmic reticulum membrane |
| D | 0016887 | molecular_function | ATP hydrolysis activity |
| D | 0034399 | cellular_component | nuclear periphery |
| D | 0034605 | biological_process | cellular response to heat |
| D | 0034975 | biological_process | protein folding in endoplasmic reticulum |
| D | 0035617 | biological_process | stress granule disassembly |
| D | 0042026 | biological_process | protein refolding |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0043335 | biological_process | protein unfolding |
| D | 0043531 | molecular_function | ADP binding |
| D | 0051082 | molecular_function | unfolded protein binding |
| D | 0051087 | molecular_function | protein-folding chaperone binding |
| D | 0070013 | cellular_component | intracellular organelle lumen |
| D | 0070370 | biological_process | cellular heat acclimation |
| D | 0072380 | cellular_component | TRC complex |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0005991 | biological_process | trehalose metabolic process |
| E | 0006457 | biological_process | protein folding |
| E | 0006620 | biological_process | post-translational protein targeting to endoplasmic reticulum membrane |
| E | 0016887 | molecular_function | ATP hydrolysis activity |
| E | 0034399 | cellular_component | nuclear periphery |
| E | 0034605 | biological_process | cellular response to heat |
| E | 0034975 | biological_process | protein folding in endoplasmic reticulum |
| E | 0035617 | biological_process | stress granule disassembly |
| E | 0042026 | biological_process | protein refolding |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0043335 | biological_process | protein unfolding |
| E | 0043531 | molecular_function | ADP binding |
| E | 0051082 | molecular_function | unfolded protein binding |
| E | 0051087 | molecular_function | protein-folding chaperone binding |
| E | 0070013 | cellular_component | intracellular organelle lumen |
| E | 0070370 | biological_process | cellular heat acclimation |
| E | 0072380 | cellular_component | TRC complex |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0005515 | molecular_function | protein binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005634 | cellular_component | nucleus |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0005991 | biological_process | trehalose metabolic process |
| F | 0006457 | biological_process | protein folding |
| F | 0006620 | biological_process | post-translational protein targeting to endoplasmic reticulum membrane |
| F | 0016887 | molecular_function | ATP hydrolysis activity |
| F | 0034399 | cellular_component | nuclear periphery |
| F | 0034605 | biological_process | cellular response to heat |
| F | 0034975 | biological_process | protein folding in endoplasmic reticulum |
| F | 0035617 | biological_process | stress granule disassembly |
| F | 0042026 | biological_process | protein refolding |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0043335 | biological_process | protein unfolding |
| F | 0043531 | molecular_function | ADP binding |
| F | 0051082 | molecular_function | unfolded protein binding |
| F | 0051087 | molecular_function | protein-folding chaperone binding |
| F | 0070013 | cellular_component | intracellular organelle lumen |
| F | 0070370 | biological_process | cellular heat acclimation |
| F | 0072380 | cellular_component | TRC complex |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue ATP A 1001 |
| Chain | Residue |
| A | VAL186 |
| A | ALA220 |
| A | ILE351 |
| A | PRO389 |
| A | LEU393 |
| A | ILE187 |
| A | GLU213 |
| A | PRO214 |
| A | GLY215 |
| A | ILE216 |
| A | GLY217 |
| A | LYS218 |
| A | THR219 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue ATP A 1002 |
| Chain | Residue |
| A | GLU579 |
| A | GLN583 |
| A | SER616 |
| A | GLY617 |
| A | SER618 |
| A | GLY619 |
| A | LYS620 |
| A | THR621 |
| A | ASN728 |
| A | PHE772 |
| A | LEU775 |
| A | ALA825 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue ATP B 1001 |
| Chain | Residue |
| B | PRO185 |
| B | VAL186 |
| B | ILE187 |
| B | PRO214 |
| B | GLY215 |
| B | ILE216 |
| B | GLY217 |
| B | LYS218 |
| B | THR219 |
| B | ALA220 |
| B | LEU355 |
| B | ASP390 |
| B | LEU393 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue ATP B 1002 |
| Chain | Residue |
| B | VAL580 |
| B | VAL581 |
| B | SER616 |
| B | GLY617 |
| B | SER618 |
| B | GLY619 |
| B | LYS620 |
| B | THR621 |
| B | GLU622 |
| B | ASN728 |
| B | ILE783 |
| B | ALA825 |
| B | ARG826 |
| B | ASN829 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | binding site for residue ATP C 1001 |
| Chain | Residue |
| C | PRO185 |
| C | VAL186 |
| C | ILE187 |
| C | PRO214 |
| C | GLY215 |
| C | GLY217 |
| C | LYS218 |
| C | THR219 |
| C | ALA220 |
| C | ILE351 |
| C | LEU393 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | binding site for residue ATP C 1002 |
| Chain | Residue |
| B | ARG765 |
| C | GLU579 |
| C | VAL580 |
| C | VAL581 |
| C | SER616 |
| C | GLY617 |
| C | SER618 |
| C | GLY619 |
| C | LYS620 |
| C | THR621 |
| C | GLU622 |
| C | ILE783 |
| C | ARG787 |
| C | ALA825 |
| C | ARG826 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | binding site for residue ATP D 901 |
| Chain | Residue |
| C | ARG765 |
| D | GLU579 |
| D | VAL580 |
| D | VAL581 |
| D | SER616 |
| D | GLY617 |
| D | SER618 |
| D | GLY619 |
| D | LYS620 |
| D | THR621 |
| D | GLU622 |
| D | LEU775 |
| D | ALA825 |
| D | ARG826 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | binding site for residue ATP D 902 |
| Chain | Residue |
| D | ILE216 |
| D | GLY217 |
| D | LYS218 |
| D | THR219 |
| D | ALA220 |
| D | ILE351 |
| D | LEU355 |
| D | PRO389 |
| D | LEU393 |
| D | ASP184 |
| D | PRO185 |
| D | VAL186 |
| D | ILE187 |
| D | ARG189 |
| D | PRO214 |
| D | GLY215 |
| site_id | AC9 |
| Number of Residues | 14 |
| Details | binding site for residue ATP E 1001 |
| Chain | Residue |
| D | ARG333 |
| D | ARG334 |
| E | ASP184 |
| E | PRO185 |
| E | VAL186 |
| E | ILE187 |
| E | GLY215 |
| E | ILE216 |
| E | GLY217 |
| E | LYS218 |
| E | THR219 |
| E | ALA220 |
| E | ILE351 |
| E | LEU393 |
| site_id | AD1 |
| Number of Residues | 15 |
| Details | binding site for residue ATP E 1002 |
| Chain | Residue |
| D | ARG765 |
| E | GLU579 |
| E | VAL580 |
| E | VAL581 |
| E | SER616 |
| E | GLY617 |
| E | SER618 |
| E | GLY619 |
| E | LYS620 |
| E | THR621 |
| E | GLU622 |
| E | ARG787 |
| E | ALA825 |
| E | ARG826 |
| E | ASN829 |
| site_id | AD2 |
| Number of Residues | 11 |
| Details | binding site for residue ATP E 1003 |
| Chain | Residue |
| E | SER306 |
| E | ARG307 |
| E | ALA330 |
| E | ARG333 |
| E | ARG334 |
| F | PRO214 |
| F | GLY215 |
| F | ILE351 |
| F | LEU355 |
| F | PRO389 |
| F | LEU393 |
| site_id | AD3 |
| Number of Residues | 15 |
| Details | binding site for residue ATP F 901 |
| Chain | Residue |
| F | VAL581 |
| F | GLN583 |
| F | SER616 |
| F | GLY617 |
| F | SER618 |
| F | GLY619 |
| F | LYS620 |
| F | THR621 |
| F | GLU622 |
| F | ASN728 |
| F | LEU775 |
| F | ILE783 |
| F | ARG787 |
| F | ALA825 |
| F | ARG826 |
| site_id | AD4 |
| Number of Residues | 38 |
| Details | binding site for Di-peptide LEU C 763 and ARG D 830 |
| Chain | Residue |
| B | LEU763 |
| B | ASN764 |
| B | ILE766 |
| B | SER767 |
| C | VAL754 |
| C | ARG759 |
| C | PRO760 |
| C | GLU761 |
| C | PHE762 |
| C | ASN764 |
| C | ARG765 |
| C | ILE766 |
| C | MET823 |
| C | ARG826 |
| C | PRO827 |
| C | LEU828 |
| C | ASN829 |
| C | LEU831 |
| C | ILE832 |
| C | GLN833 |
| C | ASN834 |
| D | VAL754 |
| D | ARG759 |
| D | PRO760 |
| D | PHE762 |
| D | ASN764 |
| D | ARG765 |
| D | ILE766 |
| D | MET823 |
| D | ARG826 |
| D | PRO827 |
| D | LEU828 |
| D | ASN829 |
| D | LEU831 |
| D | ILE832 |
| D | GLN833 |
| D | ASN834 |
| E | ARG830 |
| site_id | AD5 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide GLN D 106 and LYS C 107 |
| Chain | Residue |
| C | ILE102 |
| C | GLN103 |
| C | LYS104 |
| C | GLN105 |
| C | ASP108 |
| C | ARG148 |
| C | GLY149 |
| D | ILE102 |
| D | GLN103 |
| D | LYS104 |
| D | GLN105 |
| D | ASP108 |
| site_id | AD6 |
| Number of Residues | 12 |
| Details | binding site for Di-peptide GLN D 106 and LYS C 107 |
| Chain | Residue |
| C | ILE102 |
| C | GLN103 |
| C | LYS104 |
| C | GLN105 |
| C | ASP108 |
| C | ARG148 |
| C | GLY149 |
| D | ILE102 |
| D | GLN103 |
| D | LYS104 |
| D | GLN105 |
| D | ASP108 |
| site_id | AD7 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide GLU D 213 and ARG D 387 |
| Chain | Residue |
| D | GLY212 |
| D | PRO214 |
| D | GLY215 |
| D | ILE216 |
| D | LYS218 |
| D | GLU342 |
| D | ARG386 |
| D | LEU388 |
| D | PRO389 |
| D | ASP390 |
| D | SER391 |
| site_id | AD8 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide GLU D 213 and ARG D 387 |
| Chain | Residue |
| D | GLY212 |
| D | PRO214 |
| D | GLY215 |
| D | ILE216 |
| D | LYS218 |
| D | GLU342 |
| D | ARG386 |
| D | LEU388 |
| D | PRO389 |
| D | ASP390 |
| D | SER391 |
| site_id | AD9 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide GLU D 213 and ARG D 387 |
| Chain | Residue |
| D | GLY212 |
| D | PRO214 |
| D | GLY215 |
| D | ILE216 |
| D | LYS218 |
| D | GLU342 |
| D | ARG386 |
| D | LEU388 |
| D | PRO389 |
| D | ASP390 |
| D | SER391 |
| site_id | AE1 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide GLU D 213 and ARG D 387 |
| Chain | Residue |
| D | GLY212 |
| D | PRO214 |
| D | GLY215 |
| D | ILE216 |
| D | LYS218 |
| D | GLU342 |
| D | ARG386 |
| D | LEU388 |
| D | PRO389 |
| D | ASP390 |
| D | SER391 |
| site_id | AE2 |
| Number of Residues | 30 |
| Details | binding site for Di-peptide ILE E 204 and ASP F 397 |
| Chain | Residue |
| D | ARG202 |
| D | ILE204 |
| E | ARG202 |
| E | ARG203 |
| E | LYS205 |
| E | SER206 |
| E | TYR359 |
| E | HIS363 |
| E | LEU393 |
| E | ASP394 |
| E | LEU395 |
| E | VAL396 |
| E | ILE398 |
| E | SER399 |
| E | CYS400 |
| E | ALA401 |
| F | ARG202 |
| F | ARG203 |
| F | LYS205 |
| F | SER206 |
| F | TYR359 |
| F | HIS363 |
| F | LEU393 |
| F | ASP394 |
| F | LEU395 |
| F | VAL396 |
| F | ILE398 |
| F | SER399 |
| F | CYS400 |
| F | ALA401 |
| site_id | AE3 |
| Number of Residues | 32 |
| Details | binding site for Di-peptide LYS E 205 and ASP F 394 |
| Chain | Residue |
| D | LYS205 |
| E | ARG202 |
| E | ILE204 |
| E | SER206 |
| E | ASN207 |
| E | LEU305 |
| E | GLY308 |
| E | ARG386 |
| E | ASP390 |
| E | SER391 |
| E | ALA392 |
| E | LEU393 |
| E | LEU395 |
| E | VAL396 |
| E | ASP397 |
| E | ILE398 |
| F | VAL199 |
| F | ARG202 |
| F | ILE204 |
| F | SER206 |
| F | ASN207 |
| F | ARG333 |
| F | ARG334 |
| F | ARG386 |
| F | ASP390 |
| F | SER391 |
| F | ALA392 |
| F | LEU393 |
| F | LEU395 |
| F | VAL396 |
| F | ASP397 |
| F | ILE398 |
| site_id | AE4 |
| Number of Residues | 26 |
| Details | binding site for Di-peptide TYR E 650 and TYR D 662 |
| Chain | Residue |
| C | GLY661 |
| C | TYR662 |
| D | SER647 |
| D | GLU648 |
| D | LYS649 |
| D | ALA651 |
| D | VAL652 |
| D | SER653 |
| D | LYS654 |
| D | ALA660 |
| D | GLY661 |
| D | VAL663 |
| D | GLY664 |
| E | SER647 |
| E | GLU648 |
| E | LYS649 |
| E | ALA651 |
| E | VAL652 |
| E | SER653 |
| E | LYS654 |
| E | ALA660 |
| E | GLY661 |
| E | VAL663 |
| E | GLY664 |
| F | LYS649 |
| F | TYR650 |
| site_id | AE5 |
| Number of Residues | 37 |
| Details | binding site for Di-peptide ARG E 765 and ARG F 826 |
| Chain | Residue |
| D | ASP704 |
| D | ASN764 |
| D | ARG765 |
| E | SER609 |
| E | LEU700 |
| E | ASP704 |
| E | GLU761 |
| E | PHE762 |
| E | LEU763 |
| E | ASN764 |
| E | ILE766 |
| E | SER767 |
| E | MET823 |
| E | GLY824 |
| E | ALA825 |
| E | PRO827 |
| E | LEU828 |
| E | ASN829 |
| E | ARG830 |
| E | ATP1002 |
| F | GLN606 |
| F | SER609 |
| F | LEU700 |
| F | LEU703 |
| F | ASP704 |
| F | GLU761 |
| F | PHE762 |
| F | LEU763 |
| F | ASN764 |
| F | ILE766 |
| F | GLY824 |
| F | ALA825 |
| F | PRO827 |
| F | LEU828 |
| F | ASN829 |
| F | ARG830 |
| F | ATP901 |
| site_id | AE6 |
| Number of Residues | 37 |
| Details | binding site for Di-peptide ARG E 765 and ARG F 826 |
| Chain | Residue |
| D | ASP704 |
| D | ASN764 |
| D | ARG765 |
| E | SER609 |
| E | LEU700 |
| E | ASP704 |
| E | GLU761 |
| E | PHE762 |
| E | LEU763 |
| E | ASN764 |
| E | ILE766 |
| E | SER767 |
| E | MET823 |
| E | GLY824 |
| E | ALA825 |
| E | PRO827 |
| E | LEU828 |
| E | ASN829 |
| E | ARG830 |
| E | ATP1002 |
| F | GLN606 |
| F | SER609 |
| F | LEU700 |
| F | LEU703 |
| F | ASP704 |
| F | GLU761 |
| F | PHE762 |
| F | LEU763 |
| F | ASN764 |
| F | ILE766 |
| F | GLY824 |
| F | ALA825 |
| F | PRO827 |
| F | LEU828 |
| F | ASN829 |
| F | ARG830 |
| F | ATP901 |
| site_id | AE7 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide LYS F 205 and ARG F 333 |
| Chain | Residue |
| F | VAL199 |
| F | ARG202 |
| F | ILE204 |
| F | SER206 |
| F | ASN207 |
| F | GLY329 |
| F | ALA330 |
| F | PHE331 |
| F | GLU332 |
| F | ARG334 |
| F | PHE335 |
| site_id | AE8 |
| Number of Residues | 11 |
| Details | binding site for Di-peptide LYS F 205 and ARG F 333 |
| Chain | Residue |
| F | VAL199 |
| F | ARG202 |
| F | ILE204 |
| F | SER206 |
| F | ASN207 |
| F | GLY329 |
| F | ALA330 |
| F | PHE331 |
| F | GLU332 |
| F | ARG334 |
| F | PHE335 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1140 |
| Details | Region: {"description":"NBD2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 96 |
| Details | Motif: {"description":"Nuclear localization signal"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 84 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"14557538","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 276 |
| Details | Region: {"description":"Repeat 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01251","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
