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8G4W

Cryo-EM consensus structure of Escherichia coli que-PEC (paused elongation complex) RNA Polymerase plus preQ1 ligand

Functional Information from GO Data
ChainGOidnamespacecontents
G0003677molecular_functionDNA binding
G0003899molecular_functionDNA-directed 5'-3' RNA polymerase activity
G0006351biological_processDNA-templated transcription
G0046983molecular_functionprotein dimerization activity
H0003677molecular_functionDNA binding
H0003899molecular_functionDNA-directed 5'-3' RNA polymerase activity
H0006351biological_processDNA-templated transcription
H0046983molecular_functionprotein dimerization activity
I0000345cellular_componentcytosolic DNA-directed RNA polymerase complex
I0000428cellular_componentDNA-directed RNA polymerase complex
I0003677molecular_functionDNA binding
I0003899molecular_functionDNA-directed 5'-3' RNA polymerase activity
I0005515molecular_functionprotein binding
I0005737cellular_componentcytoplasm
I0005829cellular_componentcytosol
I0006351biological_processDNA-templated transcription
I0006352biological_processDNA-templated transcription initiation
I0006879biological_processintracellular iron ion homeostasis
I0008023cellular_componenttranscription elongation factor complex
I0009408biological_processresponse to heat
I0016020cellular_componentmembrane
I0016779molecular_functionnucleotidyltransferase activity
I0031564biological_processtranscription antitermination
I0032549molecular_functionribonucleoside binding
I0032784biological_processregulation of DNA-templated transcription elongation
I0034062molecular_function5'-3' RNA polymerase activity
I0036460biological_processcellular response to cell envelope stress
I0042128biological_processnitrate assimilation
I0044780biological_processbacterial-type flagellum assembly
I0046677biological_processresponse to antibiotic
I0048870biological_processcell motility
I0071973biological_processbacterial-type flagellum-dependent cell motility
I0090605biological_processsubmerged biofilm formation
I2000142biological_processregulation of DNA-templated transcription initiation
J0000287molecular_functionmagnesium ion binding
J0000345cellular_componentcytosolic DNA-directed RNA polymerase complex
J0000428cellular_componentDNA-directed RNA polymerase complex
J0003677molecular_functionDNA binding
J0003899molecular_functionDNA-directed 5'-3' RNA polymerase activity
J0005515molecular_functionprotein binding
J0005737cellular_componentcytoplasm
J0005829cellular_componentcytosol
J0006351biological_processDNA-templated transcription
J0006352biological_processDNA-templated transcription initiation
J0006879biological_processintracellular iron ion homeostasis
J0008023cellular_componenttranscription elongation factor complex
J0008270molecular_functionzinc ion binding
J0009408biological_processresponse to heat
J0016020cellular_componentmembrane
J0016779molecular_functionnucleotidyltransferase activity
J0031564biological_processtranscription antitermination
J0032784biological_processregulation of DNA-templated transcription elongation
J0034062molecular_function5'-3' RNA polymerase activity
J0036460biological_processcellular response to cell envelope stress
J0042128biological_processnitrate assimilation
J0044780biological_processbacterial-type flagellum assembly
J0046677biological_processresponse to antibiotic
J0046872molecular_functionmetal ion binding
J0048870biological_processcell motility
J0071973biological_processbacterial-type flagellum-dependent cell motility
J0090605biological_processsubmerged biofilm formation
J2000142biological_processregulation of DNA-templated transcription initiation
K0003677molecular_functionDNA binding
K0003899molecular_functionDNA-directed 5'-3' RNA polymerase activity
K0006351biological_processDNA-templated transcription
Functional Information from PROSITE/UniProt
site_idPS01166
Number of Residues13
DetailsRNA_POL_BETA RNA polymerases beta chain signature. GdKMAGrHGNKGV
ChainResidueDetails
IGLY1063-VAL1075

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues11
DetailsBINDING: BINDING => ECO:0000269|PubMed:32871103, ECO:0007744|PDB:4MEX, ECO:0007744|PDB:4MEY
ChainResidueDetails
JCYS70
JCYS895
JCYS898
JCYS72
JCYS85
JCYS88
JASP460
JASP462
JASP464
JCYS814
JCYS888

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000255|HAMAP-Rule:MF_01322, ECO:0000269|PubMed:18723842
ChainResidueDetails
JLYS983

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PDB entries from 2024-05-08

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