Structure of PDB 5kne Chain F

Receptor sequence
>5kneF (length=607) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
EYLSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEP
GIGKTAIIEGVAQRIIDDDVPTILQGAKLFSLDLAALGDFEERFKGVLKE
IEESKTLIVLFIDEIHMLMAANILKPALSRGQLKVIGATTNNEYRSIVEK
DGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVRILDSALVTAAQ
LAKRYLPYRRLPDSALDLVDISCAGVAVARDSKPEELDSKERQLQLIQVE
IKALERDEDADSTTKDRLKLARQKEASLQEELEPLRQRYNSMIQNVVDSD
TISETAARLTGIPVKKLSESENEKLIHMERDLSSEVVGQMDAIKAVSNAV
RLSRSGLANPRQPASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIRVDCS
ELSEKYAVSKLLGTTDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVLTVML
QMLDDGRITSGQGKTIDCSNCIVIMTSNLGAEFINSQQGSKIQESTKNLV
MGAVRQHFRPEFLNRISSIVIFNKLSRKAIHKIVDIRLKEIEERFEQNDK
HYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILKNEIK
DKETVNV
3D structure
PDB5kne Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation.
ChainF
Resolution5.64 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 ANP F P185 V186 G215 I216 G217 K218 T219 A220 P21 V22 G51 I52 G53 K54 T55 A56
BS02 ANP F V580 V581 S616 G617 S618 G619 K620 T621 E622 V336 V337 S372 G373 S374 G375 K376 T377 E378
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
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:5kne, PDBe:5kne, PDBj:5kne
PDBsum5kne
PubMed27478928
UniProtP31539|HS104_YEAST Heat shock protein 104 (Gene Name=HSP104)

[Back to BioLiP]