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4FWT

Complex structure of viral RNA polymerase form III

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0001172biological_processRNA-templated transcription
A0003723molecular_functionRNA binding
A0003746molecular_functiontranslation elongation factor activity
A0003924molecular_functionGTPase activity
A0003968molecular_functionRNA-dependent RNA polymerase activity
A0005515molecular_functionprotein binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006412biological_processtranslation
A0006414biological_processtranslational elongation
A0019079biological_processviral genome replication
A0034062molecular_function5'-3' RNA polymerase activity
A0039694biological_processviral RNA genome replication
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
A0097216molecular_functionguanosine tetraphosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE GTP A 2501
ChainResidue
ALYS908
AGLY1018
APHE1023
AGLU1026
AASP1053
AASN1077
ACA2502
GC2008
TG2101
AARG914
AILE916
AASP968
ALEU969
ASER970
AALA972
ASER973
AMET1017

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 2502
ChainResidue
AASP968
ALEU969
AASP1053
AGTP2501

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 2503
ChainResidue
AASP968
AASP1053
AASP1054
GC2008

Functional Information from PROSITE/UniProt
site_idPS00301
Number of Residues16
DetailsG_TR_1 Translational (tr)-type guanine nucleotide-binding (G) domain signature. DNapeEKaRGITIntS
ChainResidueDetails
AASP335-SER350

site_idPS01126
Number of Residues16
DetailsEF_TS_1 Elongation factor Ts signature 1. LRerTGaGMmDcKKAL
ChainResidueDetails
ALEU12-LEU27

site_idPS01127
Number of Residues11
DetailsEF_TS_2 Elongation factor Ts signature 2. EVNCQTDFVAK
ChainResidueDetails
AGLU75-LYS85

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00118
ChainResidueDetails
AGLY303
AASP365
AASN420

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylserine => ECO:0000250
ChainResidueDetails
ASER286

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-methylated lysine => ECO:0000250
ChainResidueDetails
ALYS341

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250
ChainResidueDetails
ALYS598

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250
ChainResidueDetails
ATHR667

site_idSWS_FT_FI6
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:20798060, ECO:0000269|PubMed:22245970, ECO:0000269|PubMed:22884418
ChainResidueDetails
AASP968
AASP1053
AASP1054

222415

PDB entries from 2024-07-10

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