Structure of PDB 6n8t Chain A

Receptor sequence
>6n8tA (length=848) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
QFTERALTILTLAQKLASDHQHPQLQPIHILAAFIETPEDGSVPYLQNLI
EKGRYDYDLFKKVVNRNLVRIPQQQPAPAEITPSYALGKVLQDAAKIQKQ
QKDSFIAQDHILFALFNDSSIQQIFKEAQVDIEAIKQQALELRYLSKYAI
DMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEPGIGKTAII
EGVAQRIIDDDVPTILQGAKLFSLDLAALTAGAKYKGDFEERFKGVLKEI
EESKTLIVLFIDEIHMLMGNGKDDAANILKPALSRGQLKVIGATTNNEYR
SIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRILDSAL
VTAAQLAKRYLPYRRLPDSALDLVDISCAGVAVARDSKPEELDSKERQLQ
LIQVEIKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQRYNEEKHG
HEELTQAKKKLDELENKALDAERRYDTATAADLRYFAIPDIKKQIEKLED
QVAEEERRAGANSMIQNVVDSDTISETAARLTGIPVKKLSESENEKLIHM
ERDLSSEVVGQMDAIKAVSNAVRLSRSGLANPRQPASFLFLGLSGSGKTE
LAKKVAGFLFNDEDMMIRVDCSELSEKYAVSKLLGTTAGYVGYDEGGFLT
NQLQYKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRITSGQGKTIDCSNCI
VIMTSNLGAEFINSQQGSKIQESTKNLVMGAVRQHFRPEFLNRISSIVIF
NKLSRKAIHKIVDIRLKEIEERFEQNDKHYKLNLTQEAKDFLAKYGYSDD
MGARPLNRLIQNEILNKLALRILKNEIKDKETVNVVLEECLEVLPNHE
3D structure
PDB6n8t Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation.
ChainA
Resolution7.7 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 ATP A I187 P214 G215 I216 G217 K218 T219 A220 L393 I165 P192 G193 I194 G195 K196 T197 A198 L371
BS02 ATP A V581 S616 G617 S618 G619 T621 E622 I783 R787 Y819 M823 G824 A825 V559 S594 G595 S596 G597 T599 E600 I761 R765 Y797 M801 G802 A803
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0042802 identical protein binding
GO:0043531 ADP binding
GO:0051082 unfolded protein binding
GO:0051087 protein-folding chaperone binding
Biological Process
GO:0006620 post-translational protein targeting to endoplasmic reticulum membrane
GO:0034605 cellular response to heat
GO:0034975 protein folding in endoplasmic reticulum
GO:0035617 stress granule disassembly
GO:0042026 protein refolding
GO:0043335 protein unfolding
GO:0051085 chaperone cofactor-dependent protein refolding
GO:0070370 cellular heat acclimation
GO:0070414 trehalose metabolism in response to heat stress
Cellular Component
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0034399 nuclear periphery
GO:0072380 TRC complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6n8t, PDBe:6n8t, PDBj:6n8t
PDBsum6n8t
PubMed30605683
UniProtP31539|HS104_YEAST Heat shock protein 104 (Gene Name=HSP104)

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