Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6AHF

CryoEM Reconstruction of Hsp104 N728A Hexamer

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	12
Details	binding site for residue AGS C 1001

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

site_id	AC2
Number of Residues	12
Details	binding site for residue AGS D 1001

Chain	Residue
D	VAL186
D	ILE187
D	GLU213
D	PRO214
D	GLY215
D	ILE216
D	GLY217
D	LYS218
D	ILE221
D	ILE351
D	ASP390
D	LEU393

site_id	AC3
Number of Residues	15
Details	binding site for residue AGS E 1001

Chain	Residue
D	ARG333
E	PRO185
E	VAL186
E	ILE187
E	GLY215
E	ILE216
E	GLY217
E	LYS218
E	THR219
E	ALA220
E	ASP284
E	ILE351
E	LEU355
E	PRO389
E	LEU393

site_id	AC4
Number of Residues	13
Details	binding site for residue AGS E 1002

Chain	Residue
D	GLU761
E	GLU579
E	VAL580
E	VAL581
E	LEU615
E	SER616
E	GLY617
E	SER618
E	GLY619
E	LYS620
E	THR621
E	GLU622
E	ARG826

site_id	AC5
Number of Residues	10
Details	binding site for residue AGS F 1001

Chain	Residue
F	VAL186
F	ILE187
F	GLY188
F	PRO214
F	GLY215
F	ILE216
F	GLY217
F	LYS218
F	THR219
F	ALA220

site_id	AC6
Number of Residues	11
Details	binding site for residue AGS F 1002

Chain	Residue
F	SER616
F	GLY617
F	SER618
F	LYS620
F	THR621
F	GLU622
F	ILE780
F	ILE783
F	ARG787
F	MET823
F	ALA825

site_id	AC7
Number of Residues	12
Details	binding site for Ligand TYR D 321 bound to THR D 317

Chain	Residue
D	ILE211
D	GLU285
D	ALA315
D	THR316
D	THR317
D	ASN318
D	ASN319
D	GLU320
D	ARG322
D	SER323
D	ILE324
D	VAL325

site_id	AC8
Number of Residues	12
Details	binding site for Ligand TYR D 321 bound to THR D 317

Chain	Residue
D	ILE211
D	GLU285
D	ALA315
D	THR316
D	THR317
D	ASN318
D	ASN319
D	GLU320
D	ARG322
D	SER323
D	ILE324
D	VAL325

site_id	AC9
Number of Residues	29
Details	binding site for Di-peptide ARG E 203 and TYR F 359

Chain	Residue
E	ALA201
E	ARG202
E	ILE204
E	LEU355
E	GLN356
E	PRO357
E	LYS358
E	GLU360
E	ILE361
E	HIS362
E	VAL396
E	ASP397
E	CYS400
F	ALA201
F	ARG202
F	ILE204
F	LYS205
F	SER206
F	LEU355
F	GLN356
F	PRO357
F	LYS358
F	GLU360
F	ILE361
F	HIS362
F	HIS363
F	ASP397
A	GLU874
D	ILE204

site_id	AD1
Number of Residues	26
Details	binding site for Di-peptide ILE E 204 and TYR F 359

Chain	Residue
D	ILE204
E	ARG202
E	ARG203
E	LYS205
E	LEU355
E	GLN356
E	PRO357
E	LYS358
E	GLU360
E	ILE361
E	HIS362
E	VAL396
E	ASP397
E	CYS400
F	ARG203
F	LYS205
F	ARG333
F	LEU355
F	GLN356
F	PRO357
F	LYS358
F	GLU360
F	ILE361
F	HIS362
F	HIS363
F	ASP397

site_id	AD2
Number of Residues	10
Details	binding site for Di-peptide ASP F 184 and LYS F 358

Chain	Residue
F	LYS182
F	LEU183
F	PRO185
F	VAL186
F	GLN356
F	PRO357
F	TYR359
F	GLU360
F	ILE361
F	HIS362

site_id	AD3
Number of Residues	10
Details	binding site for Di-peptide ASP F 184 and LYS F 358

Chain	Residue
F	LYS182
F	LEU183
F	PRO185
F	VAL186
F	GLN356
F	PRO357
F	TYR359
F	GLU360
F	ILE361
F	HIS362

site_id	AD4
Number of Residues	7
Details	binding site for Di-peptide ALA F 330 and ARG F 334

Chain	Residue
F	LYS205
F	ASP328
F	GLY329
F	PHE331
F	GLU332
F	ARG333
F	PHE335

site_id	AD5
Number of Residues	7
Details	binding site for Di-peptide ALA F 330 and ARG F 334

Chain	Residue
F	LYS205
F	ASP328
F	GLY329
F	PHE331
F	GLU332
F	ARG333
F	PHE335

site_id	AD6
Number of Residues	14
Details	binding site for Di-peptide PHE F 331 and PHE F 335

Chain	Residue
F	LYS205
F	SER206
F	ASN207
F	PRO208
F	VAL312
F	VAL325
F	GLU326
F	ASP328
F	GLY329
F	ALA330
F	GLU332
F	ARG333
F	ARG334
F	GLN336

site_id	AD7
Number of Residues	13
Details	binding site for Di-peptide LEU F 700 and LEU F 703

Chain	Residue
F	PRO607
F	LEU696
F	THR697
F	VAL698
F	MET699
F	GLN701
F	MET702
F	ASP704
F	ASP705
F	GLU761
F	PHE762
F	ARG765
F	ILE766

site_id	AD8
Number of Residues	13
Details	binding site for Di-peptide LEU F 700 and LEU F 703

Chain	Residue
F	PRO607
F	LEU696
F	THR697
F	VAL698
F	MET699
F	GLN701
F	MET702
F	ASP704
F	ASP705
F	GLU761
F	PHE762
F	ARG765
F	ILE766

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: 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
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_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
A	LYS442
B	LYS442
C	LYS442
D	LYS442
E	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
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)