Structure of PDB 5vy9 Chain B

Receptor sequence

>5vy9B (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

PDB

5vy9 Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104.

Chain

Resolution

6.7 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)
BS01	peptide	B	Y257 G661 V663	Y236 G640 V642
BS02	AGS	B	V186 I187 G215 G217 K218 T219 A220 I351 D390 L393	V165 I166 G194 G196 K197 T198 A199 I330 D369 L372
BS03	AGS	B	V580 V581 S616 G617 S618 G619 K620 T621 E622 D686 I783 A825 N829	V559 V560 S595 G596 S597 G598 K599 T600 E601 D665 I762 A804 N808

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

View graph for
Molecular Function

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Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:5vy9, PDBe:5vy9, PDBj:5vy9
PDBsum	5vy9
PubMed	28619716
UniProt	P31539\|HS104_YEAST Heat shock protein 104 (Gene Name=HSP104)

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