Structure of PDB 5vy8 Chain D

Receptor sequence
>5vy8D (length=705) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
YLSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEPG
IGKTAIIEGVAQRIIDDDVPTILQGAKLFSLDLAALTAGAKYKGDFEERF
KGVLKEIEESKTLIVLFIDEIHMLMGNGKDDAANILKPALSRGQLKVIGA
TTNNEYRSIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGV
RILDSALVTAAQLAKRYLPYRRLPDSALDLVDISCAGVAVARDSKPEELD
SKERQLQLIQVEIKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQR
YNEEKHGHEELTQAKKKLDELENKALDAERRYDTATAADLRYFAIPDIKK
QIEKLEDQVAEEERRAGANSMIQNVVDSDTISETAARLTGIPVKKLSESE
NEKLIHMERDLSSEVVGQMDAIKAVSNAVRLSRSGLANPRQPASFLFLGL
SGSGKTELAKKVAGFLFNDEDMMIRVDCSELSEKYAVSKLLGTTAGYVGY
DEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLTVMLQMLDDGRITSGQGKT
IDCSNCIVIMTSNLGAEFINSQQGSKIQESTKNLVMGAVRQHFRPEFLNR
ISSIVIFNKLSRKAIHKIVDIRLKEIEERFEQNDKHYKLNLTQEAKDFLA
KYGYSDDMGARPLNRLIQNEILNKLALRILKNEIKDKETVNVVLEAEECL
EVLPN
3D structure
PDB5vy8 Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104.
ChainD
Resolution5.6 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 ADP D V186 G215 G217 K218 T219 A220 P389 D390 L393 V21 G50 G52 K53 T54 A55 P224 D225 L228
BS02 ADP D V581 G617 S618 G619 K620 T621 E622 L775 I783 R787 V416 G452 S453 G454 K455 T456 E457 L610 I618 R622
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:5vy8, PDBe:5vy8, PDBj:5vy8
PDBsum5vy8
PubMed28619716
UniProtP31539|HS104_YEAST Heat shock protein 104 (Gene Name=HSP104)

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