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3MMP

Structure of the Qb replicase, an RNA-dependent RNA polymerase consisting of viral and host proteins

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0003723molecular_functionRNA binding
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0005085molecular_functionguanyl-nucleotide exchange factor activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0008270molecular_functionzinc ion binding
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0032045cellular_componentguanyl-nucleotide exchange factor complex
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
A0097216molecular_functionguanosine tetraphosphate binding
C0000166molecular_functionnucleotide binding
C0000287molecular_functionmagnesium ion binding
C0003723molecular_functionRNA binding
C0003746molecular_functiontranslation elongation factor activity
C0003924molecular_functionGTPase activity
C0005085molecular_functionguanyl-nucleotide exchange factor activity
C0005515molecular_functionprotein binding
C0005525molecular_functionGTP binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006412biological_processtranslation
C0006414biological_processtranslational elongation
C0008270molecular_functionzinc ion binding
C0016020cellular_componentmembrane
C0016787molecular_functionhydrolase activity
C0032045cellular_componentguanyl-nucleotide exchange factor complex
C0046677biological_processresponse to antibiotic
C0046872molecular_functionmetal ion binding
C0097216molecular_functionguanosine tetraphosphate binding
F0000166molecular_functionnucleotide binding
F0001172biological_processRNA-templated transcription
F0003723molecular_functionRNA binding
F0003968molecular_functionRNA-directed RNA polymerase activity
F0005515molecular_functionprotein binding
F0016740molecular_functiontransferase activity
F0016779molecular_functionnucleotidyltransferase activity
F0019079biological_processviral genome replication
F0034062molecular_function5'-3' RNA polymerase activity
F0039694biological_processviral RNA genome replication
F0046872molecular_functionmetal ion binding
G0000166molecular_functionnucleotide binding
G0001172biological_processRNA-templated transcription
G0003723molecular_functionRNA binding
G0003968molecular_functionRNA-directed RNA polymerase activity
G0005515molecular_functionprotein binding
G0016740molecular_functiontransferase activity
G0016779molecular_functionnucleotidyltransferase activity
G0019079biological_processviral genome replication
G0034062molecular_function5'-3' RNA polymerase activity
G0039694biological_processviral RNA genome replication
G0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PXN A 1394
ChainResidue
AHOH741
AHOH887
AARG1262
GPRO143
GMET148
GTYR186
GALA189

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PXN C 1394
ChainResidue
FMET148
FTYR186
CARG1262
FPRO143

Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DNapeEKaRGITIntS
ChainResidueDetails
AASP1050-SER1065

site_idPS01126
Number of Residues16
DetailsEF_TS_1 Elongation factor Ts signature 1. LRerTGaGMmDcKKAL
ChainResidueDetails
ALEU11-LEU26

site_idPS01127
Number of Residues11
DetailsEF_TS_2 Elongation factor Ts signature 2. EVNCQTDFVAK
ChainResidueDetails
AGLU74-LYS84

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsRegion: {"description":"Involved in Mg(2+) ion dislocation from EF-Tu","evidences":[{"source":"HAMAP-Rule","id":"MF_00050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues14
DetailsRegion: {"description":"G1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsRegion: {"description":"G3","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsRegion: {"description":"G4","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsRegion: {"description":"G5","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues28
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00118","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues10
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"PubMed","id":"21151122","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19150849","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24141193","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"8416965","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues264
DetailsDomain: {"description":"RdRp catalytic","evidences":[{"source":"PROSITE-ProRule","id":"PRU00539","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"20798060","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22245970","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22884418","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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