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7TNZ

Cryo-EM structure of RIG-I in complex with p1dsRNA

Functional Information from GO Data
ChainGOidnamespacecontents
A0002230biological_processpositive regulation of defense response to virus by host
A0002376biological_processimmune system process
A0002735biological_processpositive regulation of myeloid dendritic cell cytokine production
A0002753biological_processcytoplasmic pattern recognition receptor signaling pathway
A0003676molecular_functionnucleic acid binding
A0003689molecular_functionDNA clamp loader activity
A0003690molecular_functiondouble-stranded DNA binding
A0003723molecular_functionRNA binding
A0003724molecular_functionRNA helicase activity
A0003725molecular_functiondouble-stranded RNA binding
A0003727molecular_functionsingle-stranded RNA binding
A0004386molecular_functionhelicase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005525molecular_functionGTP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0005923cellular_componentbicellular tight junction
A0006338biological_processchromatin remodeling
A0008270molecular_functionzinc ion binding
A0009597biological_processdetection of virus
A0009615biological_processresponse to virus
A0010467biological_processgene expression
A0010628biological_processpositive regulation of gene expression
A0015629cellular_componentactin cytoskeleton
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0030334biological_processregulation of cell migration
A0031625molecular_functionubiquitin protein ligase binding
A0032587cellular_componentruffle membrane
A0032725biological_processpositive regulation of granulocyte macrophage colony-stimulating factor production
A0032727biological_processpositive regulation of interferon-alpha production
A0032728biological_processpositive regulation of interferon-beta production
A0032755biological_processpositive regulation of interleukin-6 production
A0032757biological_processpositive regulation of interleukin-8 production
A0032760biological_processpositive regulation of tumor necrosis factor production
A0034344biological_processregulation of type III interferon production
A0038187molecular_functionpattern recognition receptor activity
A0039529biological_processRIG-I signaling pathway
A0042802molecular_functionidentical protein binding
A0042995cellular_componentcell projection
A0043330biological_processresponse to exogenous dsRNA
A0045087biological_processinnate immune response
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046872molecular_functionmetal ion binding
A0051607biological_processdefense response to virus
A0060760biological_processpositive regulation of response to cytokine stimulus
A0061775molecular_functioncohesin loader activity
A0071360biological_processcellular response to exogenous dsRNA
A0140374biological_processantiviral innate immune response
A0140584molecular_functionchromatin extrusion motor activity
A0140588biological_processchromatin looping
A0140665molecular_functionATP-dependent H3-H4 histone complex chaperone activity
A0140849molecular_functionATP-dependent H2AZ histone chaperone activity
A1990904cellular_componentribonucleoprotein complex
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
AALA264

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01125
ChainResidueDetails
ACYS810
ACYS813
ACYS864
ACYS869

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: (Microbial infection) Phosphoserine => ECO:0000269|PubMed:34935440
ChainResidueDetails
ASER8

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: (Microbial infection) Deamidated asparagine; by herpes simplex virus 1/HHV-1 UL37 => ECO:0000269|PubMed:27866900
ChainResidueDetails
AASN495
AASN549

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CK2 => ECO:0000269|PubMed:21068236
ChainResidueDetails
ATHR770

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:21068236
ChainResidueDetails
ASER854
ASER855

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS858

site_idSWS_FT_FI8
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000305|PubMed:28469175
ChainResidueDetails
ALYS48
ALYS96

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q6Q899
ChainResidueDetails
ALYS812

site_idSWS_FT_FI10
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19484123, ECO:0000269|PubMed:24755855
ChainResidueDetails
ALYS154
ALYS164

site_idSWS_FT_FI11
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19484123, ECO:0000269|PubMed:24755855, ECO:0000269|PubMed:28469175
ChainResidueDetails
ALYS172

site_idSWS_FT_FI12
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:26471729
ChainResidueDetails
ALYS181

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PDB entries from 2024-11-06

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