Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6N8T

Hsp104DWB closed 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	0005991	biological_process	trehalose metabolic process
A	0006457	biological_process	protein folding
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	0051087	molecular_function	protein-folding chaperone binding
A	0070013	cellular_component	intracellular organelle lumen
A	0070370	biological_process	cellular heat acclimation
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	0005991	biological_process	trehalose metabolic process
B	0006457	biological_process	protein folding
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	0051087	molecular_function	protein-folding chaperone binding
B	0070013	cellular_component	intracellular organelle lumen
B	0070370	biological_process	cellular heat acclimation
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	0005991	biological_process	trehalose metabolic process
C	0006457	biological_process	protein folding
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	0051087	molecular_function	protein-folding chaperone binding
C	0070013	cellular_component	intracellular organelle lumen
C	0070370	biological_process	cellular heat acclimation
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	0005991	biological_process	trehalose metabolic process
D	0006457	biological_process	protein folding
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	0051087	molecular_function	protein-folding chaperone binding
D	0070013	cellular_component	intracellular organelle lumen
D	0070370	biological_process	cellular heat acclimation
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	0005991	biological_process	trehalose metabolic process
E	0006457	biological_process	protein folding
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	0051087	molecular_function	protein-folding chaperone binding
E	0070013	cellular_component	intracellular organelle lumen
E	0070370	biological_process	cellular heat acclimation
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	0005991	biological_process	trehalose metabolic process
F	0006457	biological_process	protein folding
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	0051087	molecular_function	protein-folding chaperone binding
F	0070013	cellular_component	intracellular organelle lumen
F	0070370	biological_process	cellular heat acclimation
F	0072380	cellular_component	TRC complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue ATP A 1001

Chain	Residue
A	PRO185
A	ALA220
A	ILE351
A	LEU393
F	GLY329
F	ARG333
A	VAL186
A	ILE187
A	PRO214
A	GLY215
A	ILE216
A	GLY217
A	LYS218
A	THR219

site_id	AC2
Number of Residues	15
Details	binding site for residue ATP A 1002

Chain	Residue
A	VAL581
A	GLN583
A	SER616
A	GLY617
A	SER618
A	GLY619
A	LYS620
A	THR621
A	GLU622
A	ILE783
A	ARG787
A	TYR819
A	MET823
A	GLY824
A	ALA825

site_id	AC3
Number of Residues	16
Details	binding site for residue ATP B 1001

Chain	Residue
A	ARG334
B	PRO185
B	VAL186
B	ILE187
B	PRO214
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 ATP B 1002

Chain	Residue
B	VAL580
B	VAL581
B	SER616
B	GLY617
B	SER618
B	GLY619
B	LYS620
B	THR621
B	GLU622
B	ASP686
B	LEU775
B	ILE783
B	ALA825
B	ASN829

site_id	AC5
Number of Residues	14
Details	binding site for residue ATP C 1001

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

site_id	AC6
Number of Residues	13
Details	binding site for residue ATP C 1002

Chain	Residue
B	ARG765
C	VAL580
C	VAL581
C	GLY617
C	SER618
C	GLY619
C	LYS620
C	THR621
C	GLU622
C	ASN728
C	LEU775
C	ILE783
C	ASN829

site_id	AC7
Number of Residues	15
Details	binding site for residue ATP D 1001

Chain	Residue
D	ASP390
D	LEU393
D	ASP184
D	PRO185
D	VAL186
D	ILE187
D	ARG189
D	PRO214
D	GLY215
D	ILE216
D	GLY217
D	LYS218
D	THR219
D	ALA220
D	ILE351

site_id	AC8
Number of Residues	14
Details	binding site for residue ATP D 1002

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

site_id	AC9
Number of Residues	13
Details	binding site for residue ATP E 1001

Chain	Residue
D	ARG334
E	PRO185
E	VAL186
E	ILE187
E	GLY215
E	ILE216
E	GLY217
E	LYS218
E	THR219
E	ALA220
E	LEU355
E	ASP390
E	LEU393

site_id	AD1
Number of Residues	16
Details	binding site for residue ATP E 1002

Chain	Residue
E	GLU579
E	VAL580
E	VAL581
E	SER616
E	GLY617
E	SER618
E	GLY619
E	LYS620
E	THR621
E	GLU622
E	ASP686
E	ASN728
E	ILE783
E	ARG787
E	ALA825
E	ARG826

site_id	AD2
Number of Residues	11
Details	binding site for residue ATP F 1001

Chain	Residue
F	VAL186
F	ILE187
F	ARG189
F	GLY215
F	ILE216
F	GLY217
F	LYS218
F	THR219
F	ALA220
F	ILE351
F	ASP390

site_id	AD3
Number of Residues	15
Details	binding site for residue ATP F 1002

Chain	Residue
F	GLU579
F	VAL580
F	VAL581
F	SER616
F	GLY617
F	SER618
F	GLY619
F	LYS620
F	THR621
F	GLU622
F	LEU775
F	ILE783
F	ARG787
F	ALA825
F	ARG826

site_id	AD4
Number of Residues	29
Details	binding site for Di-peptide GLU B 565 and LEU C 845

Chain	Residue
A	ARG595
B	SER562
B	GLU563
B	SER564
B	ASN566
B	GLU567
B	LYS568
B	ILE570
B	ARG598
B	ALA841
B	ARG843
B	ILE844
B	LYS846
B	ASN847
C	SER562
C	GLU563
C	SER564
C	ASN566
C	GLU567
C	LYS568
C	LEU569
C	ILE570
C	ALA841
C	LEU842
C	ARG843
C	ILE844
C	LYS846
C	ASN847
D	ASN847

site_id	AD5
Number of Residues	22
Details	binding site for Di-peptide GLN D 80 and GLN C 134

Chain	Residue
C	ARG59
C	TYR60
C	GLN79
C	PRO81
C	ALA82
C	PRO83
C	ALA84
C	ALA133
C	VAL135
C	ASP136
D	GLN26
D	ILE55
D	PHE65
D	GLN79
D	PRO81
D	ALA82
D	PRO83
D	PHE121
D	SER124
D	ALA133
D	VAL135
D	ASP136

site_id	AD6
Number of Residues	22
Details	binding site for Di-peptide ASP E 63 and PRO F 81

Chain	Residue
E	ASP61
E	TYR62
E	LEU64
E	PHE65
E	LYS66
E	LYS67
E	GLN79
E	GLN80
E	ALA82
E	PRO83
E	ALA84
F	GLN26
F	ASP61
F	TYR62
F	LEU64
F	PHE65
F	LYS66
F	LYS67
F	GLN80
F	ALA82
F	PRO83
F	ALA84

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	414
Details	Region: {"description":"Repeat 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01251","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	732
Details	Region: {"description":"NBD1"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1140
Details	Region: {"description":"NBD2"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	372
Details	Coiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	96
Details	Motif: {"description":"Nuclear localization signal"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	84
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	9
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	3
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	3
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"22106047","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	12
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"14557538","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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