Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8GB3

Structure of the Mycobacterium tuberculosis Hsp70 protein DnaK bound to the nucleotide exchange factor GrpE

Functional Information from GO Data
ChainGOidnamespacecontents
D0001968molecular_functionfibronectin binding
D0005524molecular_functionATP binding
D0005576cellular_componentextracellular region
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0006457biological_processprotein folding
D0009274cellular_componentpeptidoglycan-based cell wall
D0009408biological_processresponse to heat
D0009986cellular_componentcell surface
D0010756biological_processpositive regulation of plasminogen activation
D0016887molecular_functionATP hydrolysis activity
D0031072molecular_functionheat shock protein binding
D0035375molecular_functionzymogen binding
D0042026biological_processprotein refolding
D0042603cellular_componentcapsule
D0044183molecular_functionprotein folding chaperone
D0044406biological_processadhesion of symbiont to host
D0046677biological_processresponse to antibiotic
D0046688biological_processresponse to copper ion
D0046777biological_processprotein autophosphorylation
D0051082molecular_functionunfolded protein binding
D0051085biological_processchaperone cofactor-dependent protein refolding
D0071451biological_processcellular response to superoxide
D0097691cellular_componentbacterial extracellular vesicle
D0140662molecular_functionATP-dependent protein folding chaperone
D2000679biological_processpositive regulation of transcription regulatory region DNA binding
E0000774molecular_functionadenyl-nucleotide exchange factor activity
E0005737cellular_componentcytoplasm
E0006457biological_processprotein folding
E0009267biological_processcellular response to starvation
E0009274cellular_componentpeptidoglycan-based cell wall
E0042803molecular_functionprotein homodimerization activity
E0051082molecular_functionunfolded protein binding
E0051087molecular_functionprotein-folding chaperone binding
F0000774molecular_functionadenyl-nucleotide exchange factor activity
F0005737cellular_componentcytoplasm
F0006457biological_processprotein folding
F0009267biological_processcellular response to starvation
F0009274cellular_componentpeptidoglycan-based cell wall
F0042803molecular_functionprotein homodimerization activity
F0051082molecular_functionunfolded protein binding
F0051087molecular_functionprotein-folding chaperone binding
Functional Information from PROSITE/UniProt
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. VFDLGGGTfdvSLL
ChainResidueDetails
DVAL168-LEU181

site_idPS01036
Number of Residues15
DetailsHSP70_3 Heat shock hsp70 proteins family signature 3. VvLvGGsTRMPaVtD
ChainResidueDetails
DVAL310-ASP324

site_idPS01071
Number of Residues45
DetailsGRPE grpE protein signature. FDPvlHeAVqhegdggqgskpvigtvmrq.GYqlg.Eqv.LRhAlVgV
ChainResidueDetails
EPHE142-VAL186

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsMOD_RES: N-acetylthreonine => ECO:0007744|PubMed:21969609
ChainResidueDetails
ETHR2
FTHR2

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon