Structure of PDB 5vjh Chain C

Receptor sequence
>5vjhC (length=579) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
EYLSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEP
GIGKTAIIEGVAQRIIDDDVPTILQGAKLFSLDLAALTAGAKYKGDFEER
FKGVLKEIEESKTLIVLFIDEIHMLMGNGKDDAANILKPALSRGQLKVIG
ATTNNEYRSIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHG
VRILDSALVTAAQLAKRYLPYRRLPDSALDLVDISCAGVAVARDSKQNVV
DSDTISETAARLTGIPVKKLSESENEKLIHMERDLSSEVVGQMDAIKAVS
NAVRLSRSGLANPRQPASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIRV
DCSELSEKYAVSKLLGTTAGYVGYDEGGFLTNQLQYKPYSVLLFDEVEKA
HPDVLTVMLQMLDDGRITSGQGKTIDCSNCIVIMTSNLGAEFINSQQGSK
IQESTKNLVMGAVRQHFRPEFLNRISSIVIFNKLSRKAIHKIVDIRLKEI
EERFEQNDKHYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLA
LRILKNEIKDKETVNVVLEECLEVLPNHE
3D structure
PDB5vjh Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104.
ChainC
Resolution4.0 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 peptide C A255 Y257 K649 G661 Y662 V663 A91 Y93 K358 G370 Y371 V372
BS02 AGS C V186 I187 P214 G217 K218 T219 A220 I351 L393 V22 I23 P50 G53 K54 T55 A56 I187 L229
BS03 AGS C V580 V581 G617 S618 G619 K620 T621 E622 N728 A825 V289 V290 G326 S327 G328 K329 T330 E331 N437 A534
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:5vjh, PDBe:5vjh, PDBj:5vjh
PDBsum5vjh
PubMed28619716
UniProtP31539|HS104_YEAST Heat shock protein 104 (Gene Name=HSP104)

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