Structure of PDB 7to1 Chain A Binding Site BS01

Receptor Information
>7to1 Chain A (length=635) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KPRNYQLELALPAMKGKNTIICAPTGCGKTFVSLLICEHHLKKFPQGQKG
KVVFFANQIPVYEQQKSVFSKYFERHGYRVTGISGATAENVPVEQIVENN
DIIILTPQILVNNLKKGTIPSLSIFTLMIFDECHNTSKQHPYNMIMFNYL
DQKLGGSSGPLPQVIGLTASVGVGDAKNTDEALDYICKLCASLDASVIAT
VKHNLEELEQVVYKPQKFFRKVESRISDKFKYIIAQLMRDTESLAKRICK
DLENLSQIQNREFGTQKYEQWIVTVQKACMVFQMPDKDEESRICKALFLY
TSHLRKYNDALIISEHARMKDALDYLKDFFSNVRAAGFDEIEQDLTQRFE
EKLQELESVSRDPSNENPKLEDLCFILQEEYHLNPETITILFVKTRALVD
ALKNWIEGNPKLSFLKPGILDHNILIATSVAQCNLVILYEYVGRARGSKC
FLLTSNAGVIEKEQINMYKEKMMNDSILRLQTWDEAVFREKILHIQTHEK
FIRDSQEKPKPVPDKENKKLLCRKCKALACYTADVRVIEECHYTVLGDAF
KECFVSRPHPKPKQFSSFEKRAKIFCARQNCSHDWGIHVKYKTFEIPVIK
IESFVVEDIATGVQTLYSKWKDFHFEKIPFDPAEM
Ligand information
>7to1 Chain B (length=22) [Search RNA sequence] [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
ggaucgaucgaucgaucgaucc
<<<<<<<<<<..>>>>>>>>>>
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB7to1 The RIG-I receptor adopts two different conformations for distinguishing host from viral RNA ligands.
Resolution3.66 Å
Binding residue
(original residue number in PDB)		N298 I300 S325 G326 Q349 K379 Q380 Q507 Q511 V514 R546 R637 K750 C829 H830 H847 F853 S854 I875 K888 W908 K909
Binding residue
(residue number reindexed from 1)		N57 I59 S84 G85 Q108 K138 Q139 Q266 Q270 V273 R305 R396 K462 C541 H542 H559 F565 S566 I587 K600 W620 K621
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:7to1, PDBe:7to1, PDBj:7to1
PDBsum7to1
PubMed36272408
UniProtO95786|RIGI_HUMAN Antiviral innate immune response receptor RIG-I (Gene Name=RIGI)

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