Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5VJH

Closed State CryoEM Reconstruction of Hsp104:ATPyS and FITC casein

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006620	biological_process	post-translational protein targeting to endoplasmic reticulum membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0034399	cellular_component	nuclear periphery
A	0034605	biological_process	cellular response to heat
A	0034975	biological_process	protein folding in endoplasmic reticulum
A	0035617	biological_process	stress granule disassembly
A	0042026	biological_process	protein refolding
A	0042802	molecular_function	identical protein binding
A	0043335	biological_process	protein unfolding
A	0043531	molecular_function	ADP binding
A	0051082	molecular_function	unfolded protein binding
A	0051085	biological_process	chaperone cofactor-dependent protein refolding
A	0051087	molecular_function	protein-folding chaperone binding
A	0070370	biological_process	cellular heat acclimation
A	0070414	biological_process	trehalose metabolism in response to heat stress
A	0072380	cellular_component	TRC complex
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006620	biological_process	post-translational protein targeting to endoplasmic reticulum membrane
B	0016887	molecular_function	ATP hydrolysis activity
B	0034399	cellular_component	nuclear periphery
B	0034605	biological_process	cellular response to heat
B	0034975	biological_process	protein folding in endoplasmic reticulum
B	0035617	biological_process	stress granule disassembly
B	0042026	biological_process	protein refolding
B	0042802	molecular_function	identical protein binding
B	0043335	biological_process	protein unfolding
B	0043531	molecular_function	ADP binding
B	0051082	molecular_function	unfolded protein binding
B	0051085	biological_process	chaperone cofactor-dependent protein refolding
B	0051087	molecular_function	protein-folding chaperone binding
B	0070370	biological_process	cellular heat acclimation
B	0070414	biological_process	trehalose metabolism in response to heat stress
B	0072380	cellular_component	TRC complex
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006620	biological_process	post-translational protein targeting to endoplasmic reticulum membrane
C	0016887	molecular_function	ATP hydrolysis activity
C	0034399	cellular_component	nuclear periphery
C	0034605	biological_process	cellular response to heat
C	0034975	biological_process	protein folding in endoplasmic reticulum
C	0035617	biological_process	stress granule disassembly
C	0042026	biological_process	protein refolding
C	0042802	molecular_function	identical protein binding
C	0043335	biological_process	protein unfolding
C	0043531	molecular_function	ADP binding
C	0051082	molecular_function	unfolded protein binding
C	0051085	biological_process	chaperone cofactor-dependent protein refolding
C	0051087	molecular_function	protein-folding chaperone binding
C	0070370	biological_process	cellular heat acclimation
C	0070414	biological_process	trehalose metabolism in response to heat stress
C	0072380	cellular_component	TRC complex
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006620	biological_process	post-translational protein targeting to endoplasmic reticulum membrane
D	0016887	molecular_function	ATP hydrolysis activity
D	0034399	cellular_component	nuclear periphery
D	0034605	biological_process	cellular response to heat
D	0034975	biological_process	protein folding in endoplasmic reticulum
D	0035617	biological_process	stress granule disassembly
D	0042026	biological_process	protein refolding
D	0042802	molecular_function	identical protein binding
D	0043335	biological_process	protein unfolding
D	0043531	molecular_function	ADP binding
D	0051082	molecular_function	unfolded protein binding
D	0051085	biological_process	chaperone cofactor-dependent protein refolding
D	0051087	molecular_function	protein-folding chaperone binding
D	0070370	biological_process	cellular heat acclimation
D	0070414	biological_process	trehalose metabolism in response to heat stress
D	0072380	cellular_component	TRC complex
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0006620	biological_process	post-translational protein targeting to endoplasmic reticulum membrane
E	0016887	molecular_function	ATP hydrolysis activity
E	0034399	cellular_component	nuclear periphery
E	0034605	biological_process	cellular response to heat
E	0034975	biological_process	protein folding in endoplasmic reticulum
E	0035617	biological_process	stress granule disassembly
E	0042026	biological_process	protein refolding
E	0042802	molecular_function	identical protein binding
E	0043335	biological_process	protein unfolding
E	0043531	molecular_function	ADP binding
E	0051082	molecular_function	unfolded protein binding
E	0051085	biological_process	chaperone cofactor-dependent protein refolding
E	0051087	molecular_function	protein-folding chaperone binding
E	0070370	biological_process	cellular heat acclimation
E	0070414	biological_process	trehalose metabolism in response to heat stress
E	0072380	cellular_component	TRC complex
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0006620	biological_process	post-translational protein targeting to endoplasmic reticulum membrane
F	0016887	molecular_function	ATP hydrolysis activity
F	0034399	cellular_component	nuclear periphery
F	0034605	biological_process	cellular response to heat
F	0034975	biological_process	protein folding in endoplasmic reticulum
F	0035617	biological_process	stress granule disassembly
F	0042026	biological_process	protein refolding
F	0042802	molecular_function	identical protein binding
F	0043335	biological_process	protein unfolding
F	0043531	molecular_function	ADP binding
F	0051082	molecular_function	unfolded protein binding
F	0051085	biological_process	chaperone cofactor-dependent protein refolding
F	0051087	molecular_function	protein-folding chaperone binding
F	0070370	biological_process	cellular heat acclimation
F	0070414	biological_process	trehalose metabolism in response to heat stress
F	0072380	cellular_component	TRC complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue AGS A 1001

Chain	Residue
A	ASP184
A	THR219
A	ALA220
A	ILE351
A	PRO389
A	LEU393
F	ARG333
A	PRO185
A	VAL186
A	ILE187
A	PRO214
A	GLY215
A	ILE216
A	GLY217
A	LYS218

site_id	AC2
Number of Residues	12
Details	binding site for residue AGS A 1002

Chain	Residue
A	VAL580
A	VAL581
A	GLY617
A	SER618
A	GLY619
A	LYS620
A	THR621
A	GLU622
A	ILE783
A	ALA825
A	ARG826
A	ASN829

site_id	AC3
Number of Residues	18
Details	binding site for residue AGS B 1001

Chain	Residue
A	ARG307
A	ARG333
A	ARG334
B	PRO185
B	VAL186
B	ILE187
B	ARG189
B	GLY215
B	ILE216
B	GLY217
B	LYS218
B	THR219
B	ALA220
B	ILE351
B	LEU355
B	PRO389
B	ASP390
B	LEU393

site_id	AC4
Number of Residues	14
Details	binding site for residue AGS B 1002

Chain	Residue
B	GLU579
B	VAL580
B	VAL581
B	SER616
B	GLY617
B	SER618
B	GLY619
B	LYS620
B	THR621
B	GLU622
B	LEU775
B	ILE783
B	ALA825
B	ASN829

site_id	AC5
Number of Residues	15
Details	binding site for residue AGS C 1001

Chain	Residue
B	ARG334
C	ASP184
C	PRO185
C	VAL186
C	ILE187
C	ARG189
C	PRO214
C	ILE216
C	GLY217
C	LYS218
C	THR219
C	ALA220
C	ILE351
C	PRO389
C	LEU393

site_id	AC6
Number of Residues	15
Details	binding site for residue AGS C 1002

Chain	Residue
B	ARG765
C	GLU579
C	VAL580
C	VAL581
C	GLY617
C	SER618
C	GLY619
C	LYS620
C	THR621
C	GLU622
C	ASN728
C	LEU775
C	ARG787
C	ALA825
C	ASN829

site_id	AC7
Number of Residues	16
Details	binding site for residue AGS E 1001

Chain	Residue
D	GLU622
D	LEU775
D	ARG787
D	ALA825
D	ARG826
D	ASN829
C	ARG765
D	GLU579
D	VAL580
D	VAL581
D	SER616
D	GLY617
D	SER618
D	GLY619
D	LYS620
D	THR621

site_id	AC8
Number of Residues	15
Details	binding site for residue AGS E 1002

Chain	Residue
D	ARG765
E	GLU579
E	VAL580
E	VAL581
E	SER616
E	GLY617
E	SER618
E	GLY619
E	LYS620
E	THR621
E	GLU622
E	LEU775
E	ARG787
E	ALA825
E	ASN829

site_id	AC9
Number of Residues	12
Details	binding site for residue AGS F 1001

Chain	Residue
E	ARG333
F	PRO185
F	VAL186
F	ILE187
F	PRO214
F	GLY215
F	ILE216
F	GLY217
F	LYS218
F	THR219
F	ALA220
F	ILE351

site_id	AD1
Number of Residues	18
Details	binding site for residue AGS F 1002

Chain	Residue
E	GLU761
E	ARG765
F	VAL580
F	VAL581
F	LEU615
F	SER616
F	GLY617
F	SER618
F	GLY619
F	LYS620
F	THR621
F	GLU622
F	LEU775
F	ILE783
F	ARG787
F	ALA825
F	ARG826
F	ASN829

site_id	AD2
Number of Residues	16
Details	binding site for Di-peptide LYS C 205 and ARG C 333

Chain	Residue
C	ARG202
C	ILE204
C	SER206
C	ASN207
C	LEU305
C	GLY308
C	GLY329
C	ALA330
C	PHE331
C	GLU332
C	ARG334
C	PHE335
D	GLY215
D	ARG386
D	ASP390
D	ASP394

site_id	AD3
Number of Residues	27
Details	binding site for Di-peptide GLU C 326 and GLN D 712

Chain	Residue
B	GLU326
B	LYS327
C	ARG322
C	SER323
C	ILE324
C	VAL325
C	LYS327
C	ASP328
C	THR658
C	TYR665
C	GLU667
C	SER710
C	GLY711
C	GLY713
D	ARG322
D	ILE324
D	VAL325
D	LYS327
D	ASP328
D	TYR665
D	GLU667
D	SER710
D	GLY711
D	GLY713
D	LYS714
E	ASP666
E	LYS714

site_id	AD4
Number of Residues	43
Details	binding site for Di-peptide AGS D 1001 and ARG C 334

Chain	Residue
B	ARG765
C	ASN207
C	SER306
C	ALA330
C	PHE331
C	GLU332
C	ARG333
C	PHE335
C	GLU579
C	VAL580
C	VAL581
C	GLY617
C	SER618
C	GLY619
C	LYS620
C	THR621
C	GLU622
C	ASN728
C	LEU775
C	ARG787
C	ALA825
C	ASN829
D	PRO185
D	VAL186
D	ILE187
D	ARG189
D	ASN207
D	GLY215
D	ILE216
D	GLY217
D	LYS218
D	THR219
D	ALA220
D	LYS302
D	ALA330
D	PHE331
D	GLU332
D	ARG333
D	PHE335
D	ILE351
D	PRO389
D	LEU393
D	AGS1002

site_id	AD5
Number of Residues	20
Details	binding site for Di-peptide AGS D 1003 and ARG D 333

Chain	Residue
D	LYS205
D	GLY329
D	ALA330
D	PHE331
D	GLU332
D	ARG334
D	PHE335
E	VAL186
E	ILE187
E	GLY215
E	ILE216
E	GLY217
E	LYS218
E	THR219
E	ALA220
E	ILE351
E	LEU355
E	PRO389
E	ASP390
E	LEU393

site_id	AD6
Number of Residues	10
Details	binding site for Di-peptide TYR E 665 and GLN E 712

Chain	Residue
D	LYS327
E	THR658
E	ALA660
E	GLY664
E	ASP666
E	GLU667
E	SER710
E	GLY711
E	GLY713
E	LYS714

site_id	AD7
Number of Residues	24
Details	binding site for Di-peptide TYR F 650 and TYR E 662

Chain	Residue
C	GLY661
C	TYR662
D	THR659
D	GLY661
D	TYR662
E	SER647
E	GLU648
E	LYS649
E	ALA651
E	VAL652
E	SER653
E	LYS654
E	THR659
E	ALA660
E	GLY661
E	VAL663
E	GLY664
F	SER647
F	GLU648
F	LYS649
F	ALA651
F	VAL652
F	SER653
F	LYS654

Functional Information from PROSITE/UniProt

site_id	PS00870
Number of Residues	13
Details	CLPAB_1 Chaperonins clpA/B signature 1. DAANILKPaLsrG

Chain	Residue	Details
A	ASP296-GLY308

site_id	PS00871
Number of Residues	19
Details	CLPAB_2 Chaperonins clpA/B signature 2. RVDcSELsEKyAvSKLlGT

Chain	Residue	Details
A	ARG640-THR658

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000255

Chain	Residue	Details
D	GLY212
D	GLY614
E	GLY212
E	GLY614
F	GLY212
F	GLY614
A	GLY212
A	GLY614
B	GLY212
B	GLY614
C	GLY212
C	GLY614

site_id	SWS_FT_FI2
Number of Residues	6
Details	MOD_RES: N-acetylmethionine => ECO:0007744\|PubMed:22814378

Chain	Residue	Details
A	MET1
B	MET1
C	MET1
D	MET1
E	MET1
F	MET1

site_id	SWS_FT_FI3
Number of Residues	6
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18407956, ECO:0007744\|PubMed:19779198

Chain	Residue	Details
A	SER206
B	SER206
C	SER206
D	SER206
E	SER206
F	SER206

site_id	SWS_FT_FI4
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18407956

Chain	Residue	Details
D	SER306
D	SER535
E	SER306
E	SER535
F	SER306
F	SER535
A	SER306
A	SER535
B	SER306
B	SER535
C	SER306
C	SER535

site_id	SWS_FT_FI5
Number of Residues	6
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:18407956

Chain	Residue	Details
A	THR499
B	THR499
C	THR499
D	THR499
E	THR499
F	THR499

site_id	SWS_FT_FI6
Number of Residues	6
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744\|PubMed:22106047

Chain	Residue	Details
B	LYS442
E	LYS442
A	LYS442
C	LYS442
D	LYS442
F	LYS442

site_id	SWS_FT_FI7
Number of Residues	12
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:14557538

Chain	Residue	Details
D	LYS620
E	LYS620
F	LYS620
A	LYS620
B	LYS620
C	LYS620

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)