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6N8T

Hsp104DWB closed conformation

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006620biological_processpost-translational protein targeting to endoplasmic reticulum membrane
A0016887molecular_functionATP hydrolysis activity
A0034399cellular_componentnuclear periphery
A0034605biological_processcellular response to heat
A0034975biological_processprotein folding in endoplasmic reticulum
A0035617biological_processstress granule disassembly
A0042026biological_processprotein refolding
A0042802molecular_functionidentical protein binding
A0043335biological_processprotein unfolding
A0043531molecular_functionADP binding
A0051082molecular_functionunfolded protein binding
A0051085biological_processchaperone cofactor-dependent protein refolding
A0051087molecular_functionprotein-folding chaperone binding
A0070370biological_processcellular heat acclimation
A0070414biological_processtrehalose metabolism in response to heat stress
A0072380cellular_componentTRC complex
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006620biological_processpost-translational protein targeting to endoplasmic reticulum membrane
B0016887molecular_functionATP hydrolysis activity
B0034399cellular_componentnuclear periphery
B0034605biological_processcellular response to heat
B0034975biological_processprotein folding in endoplasmic reticulum
B0035617biological_processstress granule disassembly
B0042026biological_processprotein refolding
B0042802molecular_functionidentical protein binding
B0043335biological_processprotein unfolding
B0043531molecular_functionADP binding
B0051082molecular_functionunfolded protein binding
B0051085biological_processchaperone cofactor-dependent protein refolding
B0051087molecular_functionprotein-folding chaperone binding
B0070370biological_processcellular heat acclimation
B0070414biological_processtrehalose metabolism in response to heat stress
B0072380cellular_componentTRC complex
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006620biological_processpost-translational protein targeting to endoplasmic reticulum membrane
C0016887molecular_functionATP hydrolysis activity
C0034399cellular_componentnuclear periphery
C0034605biological_processcellular response to heat
C0034975biological_processprotein folding in endoplasmic reticulum
C0035617biological_processstress granule disassembly
C0042026biological_processprotein refolding
C0042802molecular_functionidentical protein binding
C0043335biological_processprotein unfolding
C0043531molecular_functionADP binding
C0051082molecular_functionunfolded protein binding
C0051085biological_processchaperone cofactor-dependent protein refolding
C0051087molecular_functionprotein-folding chaperone binding
C0070370biological_processcellular heat acclimation
C0070414biological_processtrehalose metabolism in response to heat stress
C0072380cellular_componentTRC complex
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005634cellular_componentnucleus
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0006620biological_processpost-translational protein targeting to endoplasmic reticulum membrane
D0016887molecular_functionATP hydrolysis activity
D0034399cellular_componentnuclear periphery
D0034605biological_processcellular response to heat
D0034975biological_processprotein folding in endoplasmic reticulum
D0035617biological_processstress granule disassembly
D0042026biological_processprotein refolding
D0042802molecular_functionidentical protein binding
D0043335biological_processprotein unfolding
D0043531molecular_functionADP binding
D0051082molecular_functionunfolded protein binding
D0051085biological_processchaperone cofactor-dependent protein refolding
D0051087molecular_functionprotein-folding chaperone binding
D0070370biological_processcellular heat acclimation
D0070414biological_processtrehalose metabolism in response to heat stress
D0072380cellular_componentTRC complex
E0005515molecular_functionprotein binding
E0005524molecular_functionATP binding
E0005634cellular_componentnucleus
E0005737cellular_componentcytoplasm
E0005829cellular_componentcytosol
E0006620biological_processpost-translational protein targeting to endoplasmic reticulum membrane
E0016887molecular_functionATP hydrolysis activity
E0034399cellular_componentnuclear periphery
E0034605biological_processcellular response to heat
E0034975biological_processprotein folding in endoplasmic reticulum
E0035617biological_processstress granule disassembly
E0042026biological_processprotein refolding
E0042802molecular_functionidentical protein binding
E0043335biological_processprotein unfolding
E0043531molecular_functionADP binding
E0051082molecular_functionunfolded protein binding
E0051085biological_processchaperone cofactor-dependent protein refolding
E0051087molecular_functionprotein-folding chaperone binding
E0070370biological_processcellular heat acclimation
E0070414biological_processtrehalose metabolism in response to heat stress
E0072380cellular_componentTRC complex
F0005515molecular_functionprotein binding
F0005524molecular_functionATP binding
F0005634cellular_componentnucleus
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006620biological_processpost-translational protein targeting to endoplasmic reticulum membrane
F0016887molecular_functionATP hydrolysis activity
F0034399cellular_componentnuclear periphery
F0034605biological_processcellular response to heat
F0034975biological_processprotein folding in endoplasmic reticulum
F0035617biological_processstress granule disassembly
F0042026biological_processprotein refolding
F0042802molecular_functionidentical protein binding
F0043335biological_processprotein unfolding
F0043531molecular_functionADP binding
F0051082molecular_functionunfolded protein binding
F0051085biological_processchaperone cofactor-dependent protein refolding
F0051087molecular_functionprotein-folding chaperone binding
F0070370biological_processcellular heat acclimation
F0070414biological_processtrehalose metabolism in response to heat stress
F0072380cellular_componentTRC complex
Functional Information from PDB Data
site_idAC1
Number of Residues14
Detailsbinding site for residue ATP A 1001
ChainResidue
APRO185
AALA220
AILE351
ALEU393
FGLY329
FARG333
AVAL186
AILE187
APRO214
AGLY215
AILE216
AGLY217
ALYS218
ATHR219

site_idAC2
Number of Residues15
Detailsbinding site for residue ATP A 1002
ChainResidue
AVAL581
AGLN583
ASER616
AGLY617
ASER618
AGLY619
ALYS620
ATHR621
AGLU622
AILE783
AARG787
ATYR819
AMET823
AGLY824
AALA825

site_idAC3
Number of Residues16
Detailsbinding site for residue ATP B 1001
ChainResidue
AARG334
BPRO185
BVAL186
BILE187
BPRO214
BGLY215
BILE216
BGLY217
BLYS218
BTHR219
BALA220
BILE351
BLEU355
BPRO389
BASP390
BLEU393

site_idAC4
Number of Residues14
Detailsbinding site for residue ATP B 1002
ChainResidue
BVAL580
BVAL581
BSER616
BGLY617
BSER618
BGLY619
BLYS620
BTHR621
BGLU622
BASP686
BLEU775
BILE783
BALA825
BASN829

site_idAC5
Number of Residues14
Detailsbinding site for residue ATP C 1001
ChainResidue
CPRO185
CVAL186
CILE187
CARG189
CPRO214
CGLY215
CILE216
CGLY217
CLYS218
CTHR219
CALA220
CILE351
CPRO389
CLEU393

site_idAC6
Number of Residues13
Detailsbinding site for residue ATP C 1002
ChainResidue
BARG765
CVAL580
CVAL581
CGLY617
CSER618
CGLY619
CLYS620
CTHR621
CGLU622
CASN728
CLEU775
CILE783
CASN829

site_idAC7
Number of Residues15
Detailsbinding site for residue ATP D 1001
ChainResidue
DASP390
DLEU393
DASP184
DPRO185
DVAL186
DILE187
DARG189
DPRO214
DGLY215
DILE216
DGLY217
DLYS218
DTHR219
DALA220
DILE351

site_idAC8
Number of Residues14
Detailsbinding site for residue ATP D 1002
ChainResidue
CARG765
DVAL580
DVAL581
DSER616
DGLY617
DSER618
DGLY619
DLYS620
DTHR621
DGLU622
DLEU775
DARG787
DALA825
DASN829

site_idAC9
Number of Residues13
Detailsbinding site for residue ATP E 1001
ChainResidue
DARG334
EPRO185
EVAL186
EILE187
EGLY215
EILE216
EGLY217
ELYS218
ETHR219
EALA220
ELEU355
EASP390
ELEU393

site_idAD1
Number of Residues16
Detailsbinding site for residue ATP E 1002
ChainResidue
EGLU579
EVAL580
EVAL581
ESER616
EGLY617
ESER618
EGLY619
ELYS620
ETHR621
EGLU622
EASP686
EASN728
EILE783
EARG787
EALA825
EARG826

site_idAD2
Number of Residues11
Detailsbinding site for residue ATP F 1001
ChainResidue
FVAL186
FILE187
FARG189
FGLY215
FILE216
FGLY217
FLYS218
FTHR219
FALA220
FILE351
FASP390

site_idAD3
Number of Residues15
Detailsbinding site for residue ATP F 1002
ChainResidue
FGLU579
FVAL580
FVAL581
FSER616
FGLY617
FSER618
FGLY619
FLYS620
FTHR621
FGLU622
FLEU775
FILE783
FARG787
FALA825
FARG826

site_idAD4
Number of Residues29
Detailsbinding site for Di-peptide GLU B 565 and LEU C 845
ChainResidue
AARG595
BSER562
BGLU563
BSER564
BASN566
BGLU567
BLYS568
BILE570
BARG598
BALA841
BARG843
BILE844
BLYS846
BASN847
CSER562
CGLU563
CSER564
CASN566
CGLU567
CLYS568
CLEU569
CILE570
CALA841
CLEU842
CARG843
CILE844
CLYS846
CASN847
DASN847

site_idAD5
Number of Residues22
Detailsbinding site for Di-peptide GLN D 80 and GLN C 134
ChainResidue
CARG59
CTYR60
CGLN79
CPRO81
CALA82
CPRO83
CALA84
CALA133
CVAL135
CASP136
DGLN26
DILE55
DPHE65
DGLN79
DPRO81
DALA82
DPRO83
DPHE121
DSER124
DALA133
DVAL135
DASP136

site_idAD6
Number of Residues22
Detailsbinding site for Di-peptide ASP E 63 and PRO F 81
ChainResidue
EASP61
ETYR62
ELEU64
EPHE65
ELYS66
ELYS67
EGLN79
EGLN80
EALA82
EPRO83
EALA84
FGLN26
FASP61
FTYR62
FLEU64
FPHE65
FLYS66
FLYS67
FGLN80
FALA82
FPRO83
FALA84

Functional Information from PROSITE/UniProt
site_idPS00870
Number of Residues13
DetailsCLPAB_1 Chaperonins clpA/B signature 1. DAANILKPaLsrG
ChainResidueDetails
AASP296-GLY308

site_idPS00871
Number of Residues19
DetailsCLPAB_2 Chaperonins clpA/B signature 2. RVDcSELsEKyAvSKLlGT
ChainResidueDetails
AARG640-THR658

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY212
EGLY614
FGLY212
FGLY614
AGLY614
BGLY212
BGLY614
CGLY212
CGLY614
DGLY212
DGLY614
EGLY212

site_idSWS_FT_FI2
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER206
BSER206
CSER206
DSER206
ESER206
FSER206

site_idSWS_FT_FI3
Number of Residues12
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER306
ESER535
FSER306
FSER535
ASER535
BSER306
BSER535
CSER306
CSER535
DSER306
DSER535
ESER306

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ATHR499
BTHR499
CTHR499
DTHR499
ETHR499
FTHR499

site_idSWS_FT_FI5
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS442
BLYS442
CLYS442
DLYS442
ELYS442
FLYS442

site_idSWS_FT_FI6
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:14557538
ChainResidueDetails
ELYS620
FLYS620
ALYS620
BLYS620
CLYS620
DLYS620

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PDB entries from 2024-07-24

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