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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
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
A0032045cellular_componentguanyl-nucleotide exchange factor complex
A0046677biological_processresponse to antibiotic
A0097216molecular_functionguanosine tetraphosphate 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
C0032045cellular_componentguanyl-nucleotide exchange factor complex
C0046677biological_processresponse to antibiotic
C0097216molecular_functionguanosine tetraphosphate binding
F0000166molecular_functionnucleotide binding
F0001172biological_processRNA-templated transcription
F0003723molecular_functionRNA binding
F0003968molecular_functionRNA-dependent RNA polymerase activity
F0005515molecular_functionprotein binding
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-dependent RNA polymerase activity
G0005515molecular_functionprotein binding
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
DetailsBINDING: BINDING => ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418
ChainResidueDetails
GASP274
GASP359
GASP360
FASP274
FASP359
FASP360

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545
ChainResidueDetails
ASER1001
CSER1001

site_idSWS_FT_FI3
Number of Residues10
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS1037
CLYS1294
ALYS1176
ALYS1248
ALYS1252
ALYS1294
CLYS1037
CLYS1176
CLYS1248
CLYS1252

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000269|PubMed:2022614, ECO:0000269|PubMed:389663, ECO:0000269|PubMed:6997043, ECO:0000269|PubMed:7021545
ChainResidueDetails
ALYS1056
CLYS1056

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000269|PubMed:21151122
ChainResidueDetails
ALYS1313
CLYS1313

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000305|PubMed:19150849, ECO:0000305|PubMed:24141193, ECO:0000305|PubMed:8416965
ChainResidueDetails
ATHR1382
CTHR1382

222926

PDB entries from 2024-07-24

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