Structure of PDB 5vy9 Chain F

Receptor sequence
>5vy9F (length=849) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
QFTERALTILTLAQKLASDHQHPQLQPIHILAAFIETPEDGSVPYLQNLI
EKGRYDYDLFKKVVNRNLVRIPQQQPAPAEITPSYALGKVLQDAAKIQKQ
QKDSFIAQDHILFALFNDSSIQQIFKEAQVDIEAIKQQALELRGYLSKYA
IDMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEPGIGKTAI
IEGVAQRIIDDDVPTILQGAKLFSLDLAALTAGAKYKGDFEERFKGVLKE
IEESKTLIVLFIDEIHMLMGNGKDDAANILKPALSRGQLKVIGATTNNEY
RSIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRILDSA
LVTAAQLAKRYLPYRRLPDSALDLVDISCAGVAVARDSKPEELDSKERQL
QLIQVEIKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQRYNEEKH
GHEELTQAKKKLDELENKALDAERRYDTATAADLRYFAIPDIKKQIEKLE
DQVAEEERRAGANSMIQNVVDSDTISETAARLTGIPVKKLSESENEKLIH
MERDLSSEVVGQMDAIKAVSNAVRLSRSGLANPRQPASFLFLGLSGSGKT
ELAKKVAGFLFNDEDMMIRVDCSELSEKYAVSKLLGTTAGYVGYDEGGFL
TNQLQYKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRITSGQGKTIDCSNC
IVIMTSNLGAEFINSQQGSKIQESTKNLVMGAVRQHFRPEFLNRISSIVI
FNKLSRKAIHKIVDIRLKEIEERFEQNDKHYKLNLTQEAKDFLAKYGYSD
DMGARPLNRLIQNEILNKLALRILKNEIKDKETVNVVLEECLEVLPNHE
3D structure
PDB5vy9 Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104.
ChainF
Resolution6.7 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 AGS F E332 R333 E311 R312
BS02 AGS F V186 I187 G215 I216 G217 K218 T219 I351 D390 V165 I166 G194 I195 G196 K197 T198 I330 D369
BS03 AGS F V580 V581 S616 G617 S618 G619 T621 E622 L775 I783 R787 A825 R826 V559 V560 S595 G596 S597 G598 T600 E601 L754 I762 R766 A804 R805
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:5vy9, PDBe:5vy9, PDBj:5vy9
PDBsum5vy9
PubMed28619716
UniProtP31539|HS104_YEAST Heat shock protein 104 (Gene Name=HSP104)

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