Structure of PDB 6n8t Chain E

Receptor sequence
>6n8tE (length=719) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
QFTERALTILTLAQKLASDHQHPQLQPIHILAAFIETPEDGSVPYLQNLI
EKGRYDYDLFKKVVNRNLVRIPQQQPAPAEITPSYALGKVLQDAAKIQKQ
QKDSFIAQDHILFALFNDSSIQQIFKEAQVDIEAIKQQALELRLSKYAID
MTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEPGIGKTAIIE
GVAQRIIDDDVPTILQGAKLFSLDLAALTAGAKYKGDFEERFKGVLKEIE
ESKTLIVLFIDEIHMLMGNGKDDAANILKPALSRGQLKVIGATTNNEYRS
IVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRILDSALV
TAAQLAKRYLPYRRLPDSALDLVDISCAGVAVARDSQNVVDSDTISETAA
RLTGIPVKKLSESENEKLIHMERDLSSEVVGQMDAIKAVSNAVRLSRSGL
ANPRQPASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIRVDCSELSEKYA
VSKLLGTTAGYVGYDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLTVMLQ
MLDDGRITSGQGKTIDCSNCIVIMTSNLGAEFINSQQGSKIQESTKNLVM
GAVRQHFRPEFLNRISSIVIFNKLSRKAIHKIVDIRLKEIEERFEQNDKH
YKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILKNEIKD
KETVNVVLEECLEVLPNHE
3D structure
PDB6n8t Cryo-EM Structures of the Hsp104 Protein Disaggregase Captured in the ATP Conformation.
ChainE
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 E V186 I187 G215 I216 G217 K218 T219 L355 D390 L393 V163 I164 G192 I193 G194 K195 T196 L332 D367 L370
BS02 ATP E V580 V581 S616 G617 S618 G619 K620 T621 E622 I783 R787 R826 V429 V430 S465 G466 S467 G468 K469 T470 E471 I632 R636 R675
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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