Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6N8Z

HSP104DWB extended conformation

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	13
Details	binding site for residue ATP A 1001

Chain	Residue
A	VAL186
A	ALA220
A	ILE351
A	PRO389
A	LEU393
A	ILE187
A	GLU213
A	PRO214
A	GLY215
A	ILE216
A	GLY217
A	LYS218
A	THR219

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

Chain	Residue
A	GLU579
A	GLN583
A	SER616
A	GLY617
A	SER618
A	GLY619
A	LYS620
A	THR621
A	ASN728
A	PHE772
A	LEU775
A	ALA825

site_id	AC3
Number of Residues	13
Details	binding site for residue ATP B 1001

Chain	Residue
B	PRO185
B	VAL186
B	ILE187
B	PRO214
B	GLY215
B	ILE216
B	GLY217
B	LYS218
B	THR219
B	ALA220
B	LEU355
B	ASP390
B	LEU393

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

Chain	Residue
B	VAL580
B	VAL581
B	SER616
B	GLY617
B	SER618
B	GLY619
B	LYS620
B	THR621
B	GLU622
B	ASN728
B	ILE783
B	ALA825
B	ARG826
B	ASN829

site_id	AC5
Number of Residues	11
Details	binding site for residue ATP C 1001

Chain	Residue
C	PRO185
C	VAL186
C	ILE187
C	PRO214
C	GLY215
C	GLY217
C	LYS218
C	THR219
C	ALA220
C	ILE351
C	LEU393

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

Chain	Residue
B	ARG765
C	GLU579
C	VAL580
C	VAL581
C	SER616
C	GLY617
C	SER618
C	GLY619
C	LYS620
C	THR621
C	GLU622
C	ILE783
C	ARG787
C	ALA825
C	ARG826

site_id	AC7
Number of Residues	14
Details	binding site for residue ATP D 901

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

site_id	AC8
Number of Residues	16
Details	binding site for residue ATP D 902

Chain	Residue
D	ILE216
D	GLY217
D	LYS218
D	THR219
D	ALA220
D	ILE351
D	LEU355
D	PRO389
D	LEU393
D	ASP184
D	PRO185
D	VAL186
D	ILE187
D	ARG189
D	PRO214
D	GLY215

site_id	AC9
Number of Residues	14
Details	binding site for residue ATP E 1001

Chain	Residue
D	ARG333
D	ARG334
E	ASP184
E	PRO185
E	VAL186
E	ILE187
E	GLY215
E	ILE216
E	GLY217
E	LYS218
E	THR219
E	ALA220
E	ILE351
E	LEU393

site_id	AD1
Number of Residues	15
Details	binding site for residue ATP 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	ARG787
E	ALA825
E	ARG826
E	ASN829

site_id	AD2
Number of Residues	11
Details	binding site for residue ATP E 1003

Chain	Residue
E	SER306
E	ARG307
E	ALA330
E	ARG333
E	ARG334
F	PRO214
F	GLY215
F	ILE351
F	LEU355
F	PRO389
F	LEU393

site_id	AD3
Number of Residues	15
Details	binding site for residue ATP F 901

Chain	Residue
F	VAL581
F	GLN583
F	SER616
F	GLY617
F	SER618
F	GLY619
F	LYS620
F	THR621
F	GLU622
F	ASN728
F	LEU775
F	ILE783
F	ARG787
F	ALA825
F	ARG826

site_id	AD4
Number of Residues	38
Details	binding site for Di-peptide LEU C 763 and ARG D 830

Chain	Residue
B	LEU763
B	ASN764
B	ILE766
B	SER767
C	VAL754
C	ARG759
C	PRO760
C	GLU761
C	PHE762
C	ASN764
C	ARG765
C	ILE766
C	MET823
C	ARG826
C	PRO827
C	LEU828
C	ASN829
C	LEU831
C	ILE832
C	GLN833
C	ASN834
D	VAL754
D	ARG759
D	PRO760
D	PHE762
D	ASN764
D	ARG765
D	ILE766
D	MET823
D	ARG826
D	PRO827
D	LEU828
D	ASN829
D	LEU831
D	ILE832
D	GLN833
D	ASN834
E	ARG830

site_id	AD5
Number of Residues	12
Details	binding site for Di-peptide GLN D 106 and LYS C 107

Chain	Residue
C	ILE102
C	GLN103
C	LYS104
C	GLN105
C	ASP108
C	ARG148
C	GLY149
D	ILE102
D	GLN103
D	LYS104
D	GLN105
D	ASP108

site_id	AD6
Number of Residues	12
Details	binding site for Di-peptide GLN D 106 and LYS C 107

Chain	Residue
C	ILE102
C	GLN103
C	LYS104
C	GLN105
C	ASP108
C	ARG148
C	GLY149
D	ILE102
D	GLN103
D	LYS104
D	GLN105
D	ASP108

site_id	AD7
Number of Residues	11
Details	binding site for Di-peptide GLU D 213 and ARG D 387

Chain	Residue
D	GLY212
D	PRO214
D	GLY215
D	ILE216
D	LYS218
D	GLU342
D	ARG386
D	LEU388
D	PRO389
D	ASP390
D	SER391

site_id	AD8
Number of Residues	11
Details	binding site for Di-peptide GLU D 213 and ARG D 387

Chain	Residue
D	GLY212
D	PRO214
D	GLY215
D	ILE216
D	LYS218
D	GLU342
D	ARG386
D	LEU388
D	PRO389
D	ASP390
D	SER391

site_id	AD9
Number of Residues	11
Details	binding site for Di-peptide GLU D 213 and ARG D 387

Chain	Residue
D	GLY212
D	PRO214
D	GLY215
D	ILE216
D	LYS218
D	GLU342
D	ARG386
D	LEU388
D	PRO389
D	ASP390
D	SER391

site_id	AE1
Number of Residues	11
Details	binding site for Di-peptide GLU D 213 and ARG D 387

Chain	Residue
D	GLY212
D	PRO214
D	GLY215
D	ILE216
D	LYS218
D	GLU342
D	ARG386
D	LEU388
D	PRO389
D	ASP390
D	SER391

site_id	AE2
Number of Residues	30
Details	binding site for Di-peptide ILE E 204 and ASP F 397

Chain	Residue
D	ARG202
D	ILE204
E	ARG202
E	ARG203
E	LYS205
E	SER206
E	TYR359
E	HIS363
E	LEU393
E	ASP394
E	LEU395
E	VAL396
E	ILE398
E	SER399
E	CYS400
E	ALA401
F	ARG202
F	ARG203
F	LYS205
F	SER206
F	TYR359
F	HIS363
F	LEU393
F	ASP394
F	LEU395
F	VAL396
F	ILE398
F	SER399
F	CYS400
F	ALA401

site_id	AE3
Number of Residues	32
Details	binding site for Di-peptide LYS E 205 and ASP F 394

Chain	Residue
D	LYS205
E	ARG202
E	ILE204
E	SER206
E	ASN207
E	LEU305
E	GLY308
E	ARG386
E	ASP390
E	SER391
E	ALA392
E	LEU393
E	LEU395
E	VAL396
E	ASP397
E	ILE398
F	VAL199
F	ARG202
F	ILE204
F	SER206
F	ASN207
F	ARG333
F	ARG334
F	ARG386
F	ASP390
F	SER391
F	ALA392
F	LEU393
F	LEU395
F	VAL396
F	ASP397
F	ILE398

site_id	AE4
Number of Residues	26
Details	binding site for Di-peptide TYR E 650 and TYR D 662

Chain	Residue
C	GLY661
C	TYR662
D	SER647
D	GLU648
D	LYS649
D	ALA651
D	VAL652
D	SER653
D	LYS654
D	ALA660
D	GLY661
D	VAL663
D	GLY664
E	SER647
E	GLU648
E	LYS649
E	ALA651
E	VAL652
E	SER653
E	LYS654
E	ALA660
E	GLY661
E	VAL663
E	GLY664
F	LYS649
F	TYR650

site_id	AE5
Number of Residues	37
Details	binding site for Di-peptide ARG E 765 and ARG F 826

Chain	Residue
D	ASP704
D	ASN764
D	ARG765
E	SER609
E	LEU700
E	ASP704
E	GLU761
E	PHE762
E	LEU763
E	ASN764
E	ILE766
E	SER767
E	MET823
E	GLY824
E	ALA825
E	PRO827
E	LEU828
E	ASN829
E	ARG830
E	ATP1002
F	GLN606
F	SER609
F	LEU700
F	LEU703
F	ASP704
F	GLU761
F	PHE762
F	LEU763
F	ASN764
F	ILE766
F	GLY824
F	ALA825
F	PRO827
F	LEU828
F	ASN829
F	ARG830
F	ATP901

site_id	AE6
Number of Residues	37
Details	binding site for Di-peptide ARG E 765 and ARG F 826

Chain	Residue
D	ASP704
D	ASN764
D	ARG765
E	SER609
E	LEU700
E	ASP704
E	GLU761
E	PHE762
E	LEU763
E	ASN764
E	ILE766
E	SER767
E	MET823
E	GLY824
E	ALA825
E	PRO827
E	LEU828
E	ASN829
E	ARG830
E	ATP1002
F	GLN606
F	SER609
F	LEU700
F	LEU703
F	ASP704
F	GLU761
F	PHE762
F	LEU763
F	ASN764
F	ILE766
F	GLY824
F	ALA825
F	PRO827
F	LEU828
F	ASN829
F	ARG830
F	ATP901

site_id	AE7
Number of Residues	11
Details	binding site for Di-peptide LYS F 205 and ARG F 333

Chain	Residue
F	VAL199
F	ARG202
F	ILE204
F	SER206
F	ASN207
F	GLY329
F	ALA330
F	PHE331
F	GLU332
F	ARG334
F	PHE335

site_id	AE8
Number of Residues	11
Details	binding site for Di-peptide LYS F 205 and ARG F 333

Chain	Residue
F	VAL199
F	ARG202
F	ILE204
F	SER206
F	ASN207
F	GLY329
F	ALA330
F	PHE331
F	GLU332
F	ARG334
F	PHE335

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
A	GLY212
E	GLY614
F	GLY212
F	GLY614
A	GLY614
B	GLY212
B	GLY614
C	GLY212
C	GLY614
D	GLY212
D	GLY614
E	GLY212

site_id	SWS_FT_FI2
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_FI3
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18407956

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

site_id	SWS_FT_FI4
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_FI5
Number of Residues	6
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744\|PubMed:22106047

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

site_id	SWS_FT_FI6
Number of Residues	12
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269\|PubMed:14557538

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

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