Structure of PDB 5kne Chain B

Receptor sequence
>5kneB (length=711) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
QFTERALTILTLAQKLASDHQHPQLQPIHILAAFIETPEDGSVPYLQNLI
EKGRYDYDLFKKVVNRNLVRIPQQQPAPAEITPSYALGKVLQDAAKIQKQ
QKDSFIAQDHILFALFNDSSIQQIFKEAQVDIEAIKQQALELRGNTRIDS
RGADTNTPLEYLSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIK
SNPCLIGEPGIGKTAIIEGVAQRIIDDDVPTILQGAKLFSLDLAALTGDF
EERFKGVLKEIEESKTLIVLFIDEIHMLMGAANILKPALSRGQLKVIGAT
TNNEYRSIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHGVR
ILDSALVTAAQLAKRYLPYRRLPDSALDLVDISCAGVAVARDSSMIQNVV
DSDTISETAARLTGIPVKKLSESENEKLIHMERDLSSEVVGQMDAIKAVS
NAVRLSRSGLANPRQPASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIRV
DCSELSEKYAVSKLLGTTYDEGGFLTNQLQYKPYSVLLFDEVEKAHPDVL
TVMLQMLDDGRITSGQGKTIDCSNCIVIMTSNLGAEFINSQQGSKIQEST
KNLVMGAVRQHFRPEFLNRISSIVIFNKLSRKAIHKIVDIRLKEIEERFE
QNDKHYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLALRILK
NEIKDKETVNV
3D structure
PDB5kne Spiral architecture of the Hsp104 disaggregase reveals the basis for polypeptide translocation.
ChainB
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 B V186 I187 G215 I216 G217 K218 T219 A220 V181 I182 G210 I211 G212 K213 T214 A215
BS02 ANP B E579 V580 S616 G617 S618 G619 K620 T621 E438 V439 S475 G476 S477 G478 K479 T480
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]