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5VYA

S. cerevisiae Hsp104:casein complex, Extended 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 Residues12
Detailsbinding site for residue AGS A 1001
ChainResidue
AASP184
AGLU223
AILE351
ALEU393
APRO185
AVAL186
AGLY215
AILE216
AGLY217
ALYS218
ATHR219
AALA220

site_idAC2
Number of Residues15
Detailsbinding site for residue AGS A 1002
ChainResidue
AGLU579
AVAL580
AGLN583
AGLY617
ASER618
AGLY619
ALYS620
ATHR621
AGLU622
AASN728
ALEU775
AILE783
AARG787
AALA825
AARG826

site_idAC3
Number of Residues16
Detailsbinding site for residue AGS B 1001
ChainResidue
AILE204
AARG333
AARG334
BPRO185
BVAL186
BILE187
BPRO214
BGLY215
BILE216
BGLY217
BLYS218
BTHR219
BALA220
BLEU355
BASP390
BLEU393

site_idAC4
Number of Residues15
Detailsbinding site for residue AGS B 1002
ChainResidue
AARG765
BVAL580
BVAL581
BSER616
BGLY617
BSER618
BGLY619
BLYS620
BTHR621
BGLU622
BASN728
BILE783
BALA825
BARG826
BASN829

site_idAC5
Number of Residues13
Detailsbinding site for residue AGS C 1001
ChainResidue
BILE204
BARG334
CPRO185
CVAL186
CILE187
CPRO214
CGLY215
CGLY217
CLYS218
CTHR219
CALA220
CILE351
CLEU393

site_idAC6
Number of Residues15
Detailsbinding site for residue AGS C 1002
ChainResidue
BARG765
CGLU579
CVAL580
CVAL581
CSER616
CGLY617
CSER618
CGLY619
CLYS620
CTHR621
CGLU622
CILE783
CARG787
CALA825
CARG826

site_idAC7
Number of Residues19
Detailsbinding site for residue AGS D 1001
ChainResidue
DTHR219
DALA220
DILE351
DLEU355
DPRO389
DLEU393
CILE204
CARG333
CARG334
DASP184
DPRO185
DVAL186
DILE187
DARG189
DPRO214
DGLY215
DILE216
DGLY217
DLYS218

site_idAC8
Number of Residues15
Detailsbinding site for residue AGS E 1001
ChainResidue
DARG307
DARG333
DARG334
EASP184
EPRO185
EVAL186
EILE187
EGLY215
EILE216
EGLY217
ELYS218
ETHR219
EALA220
EILE351
ELEU393

site_idAC9
Number of Residues15
Detailsbinding site for residue AGS E 1002
ChainResidue
DARG765
EGLU579
EVAL580
EVAL581
ESER616
EGLY617
ESER618
EGLY619
ELYS620
ETHR621
EGLU622
EARG787
EALA825
EARG826
EASN829

site_idAD1
Number of Residues15
Detailsbinding site for residue AGS F 1002
ChainResidue
EARG765
FGLU579
FVAL580
FVAL581
FGLN583
FSER616
FGLY617
FSER618
FGLY619
FLYS620
FTHR621
FGLU622
FILE783
FARG787
FARG826

site_idAD2
Number of Residues21
Detailsbinding site for Di-peptide AGS C 1003 and ARG C 765
ChainResidue
CLEU700
CASP704
CGLU761
CPHE762
CLEU763
CASN764
CILE766
CSER767
DGLU579
DVAL580
DVAL581
DSER616
DGLY617
DSER618
DGLY619
DLYS620
DTHR621
DGLU622
DLEU775
DALA825
DARG826

site_idAD3
Number of Residues11
Detailsbinding site for Di-peptide GLU D 213 and ARG D 387
ChainResidue
DGLY212
DPRO214
DGLY215
DILE216
DLYS218
DGLU342
DARG386
DLEU388
DPRO389
DASP390
DSER391

site_idAD4
Number of Residues11
Detailsbinding site for Di-peptide GLU D 213 and ARG D 387
ChainResidue
DGLY212
DPRO214
DGLY215
DILE216
DLYS218
DGLU342
DARG386
DLEU388
DPRO389
DASP390
DSER391

site_idAD5
Number of Residues11
Detailsbinding site for Di-peptide GLU D 213 and ARG D 387
ChainResidue
DGLY212
DPRO214
DGLY215
DILE216
DLYS218
DGLU342
DARG386
DLEU388
DPRO389
DASP390
DSER391

site_idAD6
Number of Residues11
Detailsbinding site for Di-peptide GLU D 213 and ARG D 387
ChainResidue
DGLY212
DPRO214
DGLY215
DILE216
DLYS218
DGLU342
DARG386
DLEU388
DPRO389
DASP390
DSER391

site_idAD7
Number of Residues20
Detailsbinding site for Di-peptide AGS E 1002 and ARG E 334
ChainResidue
EASN207
ELEU305
EALA330
EPHE331
EGLU332
EARG333
EPHE335
FASP184
FPRO185
FVAL186
FILE187
FARG189
FPRO214
FGLY215
FLYS218
FTHR219
FALA220
FGLU223
FILE351
FLEU355

site_idAD8
Number of Residues11
Detailsbinding site for Di-peptide LYS F 205 and ARG F 333
ChainResidue
FVAL199
FARG202
FILE204
FSER206
FASN207
FGLY329
FALA330
FPHE331
FGLU332
FARG334
FPHE335

site_idAD9
Number of Residues11
Detailsbinding site for Di-peptide LYS F 205 and ARG F 333
ChainResidue
FVAL199
FARG202
FILE204
FSER206
FASN207
FGLY329
FALA330
FPHE331
FGLU332
FARG334
FPHE335

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: N-acetylmethionine => ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1
BMET1
CMET1
DMET1
EMET1
FMET1

site_idSWS_FT_FI3
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER206
BSER206
CSER206
DSER206
ESER206
FSER206

site_idSWS_FT_FI4
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_FI5
Number of Residues6
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ATHR499
BTHR499
CTHR499
DTHR499
ETHR499
FTHR499

site_idSWS_FT_FI6
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_FI7
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 2024-07-17

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