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7KRT

Restraining state of a truncated Hsp70 DnaK

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006260biological_processDNA replication
A0006457biological_processprotein folding
A0008270molecular_functionzinc ion binding
A0009408biological_processresponse to heat
A0016020cellular_componentmembrane
A0016234cellular_componentinclusion body
A0016887molecular_functionATP hydrolysis activity
A0016989molecular_functionsigma factor antagonist activity
A0031072molecular_functionheat shock protein binding
A0032991cellular_componentprotein-containing complex
A0034620biological_processcellular response to unfolded protein
A0042026biological_processprotein refolding
A0043335biological_processprotein unfolding
A0043531molecular_functionADP binding
A0044183molecular_functionprotein folding chaperone
A0045892biological_processnegative regulation of DNA-templated transcription
A0051082molecular_functionunfolded protein binding
A0051085biological_processchaperone cofactor-dependent protein refolding
A0051087molecular_functionprotein-folding chaperone binding
A0065003biological_processprotein-containing complex assembly
A0140662molecular_functionATP-dependent protein folding chaperone
A1990169biological_processstress response to copper ion
B0005515molecular_functionprotein binding
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006260biological_processDNA replication
B0006457biological_processprotein folding
B0008270molecular_functionzinc ion binding
B0009408biological_processresponse to heat
B0016020cellular_componentmembrane
B0016234cellular_componentinclusion body
B0016887molecular_functionATP hydrolysis activity
B0016989molecular_functionsigma factor antagonist activity
B0031072molecular_functionheat shock protein binding
B0032991cellular_componentprotein-containing complex
B0034620biological_processcellular response to unfolded protein
B0042026biological_processprotein refolding
B0043335biological_processprotein unfolding
B0043531molecular_functionADP binding
B0044183molecular_functionprotein folding chaperone
B0045892biological_processnegative regulation of DNA-templated transcription
B0051082molecular_functionunfolded protein binding
B0051085biological_processchaperone cofactor-dependent protein refolding
B0051087molecular_functionprotein-folding chaperone binding
B0065003biological_processprotein-containing complex assembly
B0140662molecular_functionATP-dependent protein folding chaperone
B1990169biological_processstress response to copper ion
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006260biological_processDNA replication
C0006457biological_processprotein folding
C0008270molecular_functionzinc ion binding
C0009408biological_processresponse to heat
C0016020cellular_componentmembrane
C0016234cellular_componentinclusion body
C0016887molecular_functionATP hydrolysis activity
C0016989molecular_functionsigma factor antagonist activity
C0031072molecular_functionheat shock protein binding
C0032991cellular_componentprotein-containing complex
C0034620biological_processcellular response to unfolded protein
C0042026biological_processprotein refolding
C0043335biological_processprotein unfolding
C0043531molecular_functionADP binding
C0044183molecular_functionprotein folding chaperone
C0045892biological_processnegative regulation of DNA-templated transcription
C0051082molecular_functionunfolded protein binding
C0051085biological_processchaperone cofactor-dependent protein refolding
C0051087molecular_functionprotein-folding chaperone binding
C0065003biological_processprotein-containing complex assembly
C0140662molecular_functionATP-dependent protein folding chaperone
C1990169biological_processstress response to copper ion
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006260biological_processDNA replication
D0006457biological_processprotein folding
D0008270molecular_functionzinc ion binding
D0009408biological_processresponse to heat
D0016020cellular_componentmembrane
D0016234cellular_componentinclusion body
D0016887molecular_functionATP hydrolysis activity
D0016989molecular_functionsigma factor antagonist activity
D0031072molecular_functionheat shock protein binding
D0032991cellular_componentprotein-containing complex
D0034620biological_processcellular response to unfolded protein
D0042026biological_processprotein refolding
D0043335biological_processprotein unfolding
D0043531molecular_functionADP binding
D0044183molecular_functionprotein folding chaperone
D0045892biological_processnegative regulation of DNA-templated transcription
D0051082molecular_functionunfolded protein binding
D0051085biological_processchaperone cofactor-dependent protein refolding
D0051087molecular_functionprotein-folding chaperone binding
D0065003biological_processprotein-containing complex assembly
D0140662molecular_functionATP-dependent protein folding chaperone
D1990169biological_processstress response to copper ion
Functional Information from PROSITE/UniProt
site_idPS00297
Number of Residues8
DetailsHSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTnS
ChainResidueDetails
AILE7-SER14

site_idPS00329
Number of Residues14
DetailsHSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGAfdiSII
ChainResidueDetails
AVAL192-ILE205

site_idPS01036
Number of Residues15
DetailsHSP70_3 Heat shock hsp70 proteins family signature 3. ViLvGGqTRMPmVqK
ChainResidueDetails
AVAL337-LYS351

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS70
BLYS502
BLYS528
BLYS587
CLYS70
CLYS246
CLYS359
CLYS502
CLYS528
CLYS587
DLYS70
ALYS246
DLYS246
DLYS359
DLYS502
DLYS528
DLYS587
ALYS359
ALYS502
ALYS528
ALYS587
BLYS70
BLYS246
BLYS359

site_idSWS_FT_FI2
Number of Residues12
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
ALYS109
DLYS109
DLYS421
DLYS556
ALYS421
ALYS556
BLYS109
BLYS421
BLYS556
CLYS109
CLYS421
CLYS556

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:1835085, ECO:0000269|PubMed:8206983
ChainResidueDetails
AALA199
BALA199
CALA199
DALA199

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS245
ALYS304
BLYS245
BLYS304
CLYS245
CLYS304
DLYS245
DLYS304

223532

PDB entries from 2024-08-07

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