Structure of PDB 5vjh Chain D

Receptor sequence

>5vjhD (length=579) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]

EYLSKYAIDMTEQARQGKLDPVIGREEEIRSTIRVLARRIKSNPCLIGEP
GIGKTAIIEGVAQRIIDDDVPTILQGAKLFSLDLAALTAGAKYKGDFEER
FKGVLKEIEESKTLIVLFIDEIHMLMGNGKDDAANILKPALSRGQLKVIG
ATTNNEYRSIVEKDGAFERRFQKIEVAEPSVRQTVAILRGLQPKYEIHHG
VRILDSALVTAAQLAKRYLPYRRLPDSALDLVDISCAGVAVARDSKQNVV
DSDTISETAARLTGIPVKKLSESENEKLIHMERDLSSEVVGQMDAIKAVS
NAVRLSRSGLANPRQPASFLFLGLSGSGKTELAKKVAGFLFNDEDMMIRV
DCSELSEKYAVSKLLGTTAGYVGYDEGGFLTNQLQYKPYSVLLFDEVEKA
HPDVLTVMLQMLDDGRITSGQGKTIDCSNCIVIMTSNLGAEFINSQQGSK
IQESTKNLVMGAVRQHFRPEFLNRISSIVIFNKLSRKAIHKIVDIRLKEI
EERFEQNDKHYKLNLTQEAKDFLAKYGYSDDMGARPLNRLIQNEILNKLA
LRILKNEIKDKETVNVVLEECLEVLPNHE

3D structure

PDB

5vjh Ratchet-like polypeptide translocation mechanism of the AAA+ disaggregase Hsp104.

Chain

Resolution

4.0 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)
BS01	peptide	D	A255 Y257 K649 G661 Y662 V663	A91 Y93 K358 G370 Y371 V372
BS02	AGS	D	V186 I187 G215 G217 K218 T219 A220 I351 L393	V22 I23 G51 G53 K54 T55 A56 I187 L229
BS03	AGS	D	R333 R334	R169 R170
BS04	AGS	D	V580 V581 S616 G617 S618 G619 K620 T621 E622 R787 A825 R826	V289 V290 S325 G326 S327 G328 K329 T330 E331 R496 A534 R535

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:5vjh, PDBe:5vjh, PDBj:5vjh
PDBsum	5vjh
PubMed	28619716
UniProt	P31539\|HS104_YEAST Heat shock protein 104 (Gene Name=HSP104)

[Back to BioLiP]