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1DKG

CRYSTAL STRUCTURE OF THE NUCLEOTIDE EXCHANGE FACTOR GRPE BOUND TO THE ATPASE DOMAIN OF THE MOLECULAR CHAPERONE DNAK

Functional Information from GO Data
ChainGOidnamespacecontents
A0000774molecular_functionadenyl-nucleotide exchange factor activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006457biological_processprotein folding
A0009408biological_processresponse to heat
A0019904molecular_functionprotein domain specific binding
A0030150biological_processprotein import into mitochondrial matrix
A0032991cellular_componentprotein-containing complex
A0042803molecular_functionprotein homodimerization activity
A0043335biological_processprotein unfolding
A0051082molecular_functionunfolded protein binding
A0051085biological_processchaperone cofactor-dependent protein refolding
A0051087molecular_functionprotein-folding chaperone binding
A0065003biological_processprotein-containing complex assembly
B0000774molecular_functionadenyl-nucleotide exchange factor activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006457biological_processprotein folding
B0009408biological_processresponse to heat
B0019904molecular_functionprotein domain specific binding
B0030150biological_processprotein import into mitochondrial matrix
B0032991cellular_componentprotein-containing complex
B0042803molecular_functionprotein homodimerization activity
B0043335biological_processprotein unfolding
B0051082molecular_functionunfolded protein binding
B0051085biological_processchaperone cofactor-dependent protein refolding
B0051087molecular_functionprotein-folding chaperone binding
B0065003biological_processprotein-containing complex assembly
D0005524molecular_functionATP binding
D0140662molecular_functionATP-dependent protein folding chaperone
Functional Information from PROSITE/UniProt
site_idPS01071
Number of Residues44
DetailsGRPE grpE protein signature. LDPnvHqAIamvesddvapgnvlgimqk..GYtln.Grt.IRaAmVtV
ChainResidueDetails
ALEU149-VAL192

site_idPS00297
Number of Residues8
DetailsHSP70_1 Heat shock hsp70 proteins family signature 1. IDLGTTnS
ChainResidueDetails
DILE7-SER14

site_idPS00329
Number of Residues14
DetailsHSP70_2 Heat shock hsp70 proteins family signature 2. VYDLGGGTfdiSII
ChainResidueDetails
DVAL192-ILE205

site_idPS01036
Number of Residues15
DetailsHSP70_3 Heat shock hsp70 proteins family signature 3. ViLvGGqTRMPmVqK
ChainResidueDetails
DVAL337-LYS351

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
DARG71
DASP247
DGLU360

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842
ChainResidueDetails
DMET110

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:1835085, ECO:0000269|PubMed:8206983
ChainResidueDetails
DPHE200

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
DLYS246
DLEU305

218853

PDB entries from 2024-04-24

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