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4B9Q

Open conformation of ATP-bound Hsp70 homolog 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 PDB Data
site_idAC1
Number of Residues28
DetailsBINDING SITE FOR RESIDUE ATP A 700
ChainResidue
AGLY10
AGLY229
AGLU267
ALYS270
AILE271
ASER274
AGLY341
AGLY342
AGLN343
AARG345
AMG701
ATHR11
AHOH2006
AHOH2008
AHOH2009
AHOH2079
AHOH2083
AHOH2084
AHOH2089
AHOH2114
AHOH2117
ATHR12
AASN13
ALYS70
AGLY196
AGLY197
AGLY198
AALA199

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 701
ChainResidue
AATP700
AHOH2006
AHOH2008
AHOH2079
AHOH2084

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ATP B 700
ChainResidue
BGLY10
BTHR11
BTHR12
BASN13
BLYS70
BGLY196
BGLY197
BGLY198
BALA199
BGLY229
BGLU267
BLYS270
BILE271
BSER274
BGLY341
BGLY342
BGLN343
BARG345
BMG701
BHOH2005
BHOH2006
BHOH2078
BHOH2082
BHOH2088
BHOH2119
BHOH2120

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 701
ChainResidue
BATP700
BHOH2004
BHOH2005
BHOH2078
BHOH2082

site_idAC5
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ATP C 700
ChainResidue
CGLY10
CTHR11
CTHR12
CASN13
CLYS70
CGLY196
CGLY197
CGLY198
CALA199
CGLY229
CGLU267
CLYS270
CILE271
CSER274
CGLY341
CGLY342
CGLN343
CARG345
CMG701
CHOH2002
CHOH2003
CHOH2004
CHOH2072
CHOH2075
CHOH2081
CHOH2094

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 701
ChainResidue
CATP700
CHOH2002
CHOH2003
CHOH2072
CHOH2075

site_idAC7
Number of Residues25
DetailsBINDING SITE FOR RESIDUE ATP D 700
ChainResidue
DLYS70
DGLY196
DGLY197
DGLY198
DALA199
DGLY229
DGLU267
DLYS270
DILE271
DSER274
DGLY341
DGLY342
DGLN343
DARG345
DMG701
DHOH2002
DHOH2003
DHOH2049
DHOH2052
DHOH2053
DHOH2065
DGLY10
DTHR11
DTHR12
DASN13

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG D 701
ChainResidue
DATP700
DHOH2002
DHOH2003
DHOH2049
DHOH2053

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

224931

PDB entries from 2024-09-11

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