Structure of PDB 7to0 Chain A Binding Site BS02

Receptor Information
>7to0 Chain A (length=682) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
FKPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQK
GKVVFFANQIPVYEQQKSVFSKYFERHGYRVTGISGATAENVPVEQIVEN
NDIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNY
LDQKLGGSSGPLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIA
TVKHNLEELEQVVYKPQKFFRKVESRISDKFKYIIAQLMRDTESLAKRIC
KDLENLSQIQNREFGTQKYEQWIVTVQKACMVFQMPDKDEESRICKALFL
YTSHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRF
EEKLQELESVSRDPSNENPKLEDLCFILQEEYHLNPETITILFVKTRALV
DALKNWIEGNPKLSFLKPGILTGRGKTNQNTGMTLPAQKCILDAFKASGD
HNILIATSVADEGIDIAQCNLVILYEYVGNVIKMIQTRGRGRARGSKCFL
LTSNAGVIEKEQINMYKEKMMNDSILRLQTWDEAVFREKILHIQTHEKFI
RDSQEKPKPVPDKENKKLLCRKCKALACYTADVRVIEECHYTVLGDAFKE
CFVSRPHPKPKQFSSFEKRAKIFCARQNCSHDWGIHVKYKTFEIPVIKIE
SFVVEDIATGVQTLYSKWKDFHFEKIPFDPAE
Ligand information
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB7to0 The RIG-I receptor adopts two different conformations for distinguishing host from viral RNA ligands.
Resolution3.5 Å
Binding residue
(original residue number in PDB)		N298 Q299 I300 Q349 I350 E510 Q511 V514 R546 K635 R637 T662 R664 T697 V699 E702 F853
Binding residue
(residue number reindexed from 1)		N58 Q59 I60 Q109 I110 E270 Q271 V274 R306 K395 R397 T422 R424 T457 V459 E462 F613
Enzymatic activity
Enzyme Commision number 3.6.4.13: RNA helicase.
Gene Ontology
Molecular Function
GO:0003676 nucleic acid binding
GO:0003690 double-stranded DNA binding
GO:0003723 RNA binding
GO:0003724 RNA helicase activity
GO:0003725 double-stranded RNA binding
GO:0003727 single-stranded RNA binding
GO:0004386 helicase activity
GO:0005515 protein binding
GO:0005524 ATP binding
GO:0005525 GTP binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0016887 ATP hydrolysis activity
GO:0031625 ubiquitin protein ligase binding
GO:0038187 pattern recognition receptor activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0002230 positive regulation of defense response to virus by host
GO:0002376 immune system process
GO:0002735 positive regulation of myeloid dendritic cell cytokine production
GO:0002753 cytoplasmic pattern recognition receptor signaling pathway
GO:0009597 detection of virus
GO:0009615 response to virus
GO:0010467 gene expression
GO:0010628 positive regulation of gene expression
GO:0030334 regulation of cell migration
GO:0032725 positive regulation of granulocyte macrophage colony-stimulating factor production
GO:0032727 positive regulation of interferon-alpha production
GO:0032728 positive regulation of interferon-beta production
GO:0032755 positive regulation of interleukin-6 production
GO:0032757 positive regulation of interleukin-8 production
GO:0032760 positive regulation of tumor necrosis factor production
GO:0034344 regulation of type III interferon production
GO:0039529 RIG-I signaling pathway
GO:0043330 response to exogenous dsRNA
GO:0045087 innate immune response
GO:0045944 positive regulation of transcription by RNA polymerase II
GO:0051607 defense response to virus
GO:0060760 positive regulation of response to cytokine stimulus
GO:0071360 cellular response to exogenous dsRNA
GO:0140374 antiviral innate immune response
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0005856 cytoskeleton
GO:0005886 plasma membrane
GO:0005923 bicellular tight junction
GO:0015629 actin cytoskeleton
GO:0032587 ruffle membrane
GO:0042995 cell projection
GO:1990904 ribonucleoprotein complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7to0, PDBe:7to0, PDBj:7to0
PDBsum7to0
PubMed36272408
UniProtO95786|RIGI_HUMAN Antiviral innate immune response receptor RIG-I (Gene Name=RIGI)

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