Structure of PDB 6n8v Chain F

Receptor sequence
>6n8vF (length=710) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
QFTERALTILTLAQKLASDHQHPQLQPIHILAAFIETPEDGSVPYLQNLI
EKGRYDYDLFKKVVNRNLVRIPQQQPAPAEITPSYALGKVLQDAAKIQKQ
QKDSFIAQDHILFALFNDSSIQQIFKEAQVDIEAIKQQALELRGNTRIDS
RGADTNTPLEYLSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIK
SNPCLIGEPGIGKTAIIEGVAQRIIDDDVPTILQGAKLFSLDLAALGDFE
ERFKGVLKEIEESKTLIVLFIDEIHMLMAANILKPALSRGQLKVIGATTN
NEYRSIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRIL
DSALVTAAQLAKRYLPYRRLPDSALDLVDISCAGVAVARDSKPSMIQNVV
DSDTISETAARLTGIPVKKLSESENEKLIHMERDLSSEVVGQMDAIKAVS
NAVRLSRSGLANPRQPASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIRV
DCSELSEKYAVSKLLGTTDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLT
VMLQMLDDGRITSGQGKTIDCSNCIVIMTSNLGAEFINSQQGSKIQESTK
NLVMGAVRQHFRPEFLNRISSIVIFNKLSRKAIHKIVDIRLKEIEERFEQ
NDKHYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILKN
EIKDKETVNV
3D structure
PDB6n8v Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation.
ChainF
Resolution9.3 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 F P185 V186 G215 I216 G217 K218 T219 A220 P180 V181 G210 I211 G212 K213 T214 A215
BS02 ATP F V580 V581 S616 G617 S618 G619 K620 T621 E622 V439 V440 S475 G476 S477 G478 K479 T480 E481
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:6n8v, PDBe:6n8v, PDBj:6n8v
PDBsum6n8v
PubMed30605683
UniProtP31539|HS104_YEAST Heat shock protein 104 (Gene Name=HSP104)

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