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6GKM

CryoEM structure of the MDA5-dsRNA filament in complex with ATP (10 mM)

Functional Information from GO Data
ChainGOidnamespacecontents
A0002376biological_processimmune system process
A0003677molecular_functionDNA 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
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0008270molecular_functionzinc ion binding
A0009615biological_processresponse to virus
A0016787molecular_functionhydrolase activity
A0016887molecular_functionATP hydrolysis activity
A0016925biological_processprotein sumoylation
A0019904molecular_functionprotein domain specific binding
A0032727biological_processpositive regulation of interferon-alpha production
A0032728biological_processpositive regulation of interferon-beta production
A0032755biological_processpositive regulation of interleukin-6 production
A0032760biological_processpositive regulation of tumor necrosis factor production
A0038187molecular_functionpattern recognition receptor activity
A0039530biological_processMDA-5 signaling pathway
A0042802molecular_functionidentical protein binding
A0043021molecular_functionribonucleoprotein complex binding
A0045071biological_processnegative regulation of viral genome replication
A0045087biological_processinnate immune response
A0046872molecular_functionmetal ion binding
A0051259biological_processprotein complex oligomerization
A0051607biological_processdefense response to virus
A0060337biological_processtype I interferon-mediated signaling pathway
A0060760biological_processpositive regulation of response to cytokine stimulus
A0071360biological_processcellular response to exogenous dsRNA
A0098586biological_processcellular response to virus
A0140374biological_processantiviral innate immune response
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1101
ChainResidue
ACYS907
ACYS910
ACYS962
ACYS964

site_idAC2
Number of Residues7
Detailsbinding site for residue ATP A 1102
ChainResidue
ATHR337
AARG338
AARG310
AGLY333
ASER334
AGLY335
ALYS336

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU01125
ChainResidueDetails
ALYS925
AHIS928
APRO980
ALEU982

site_idSWS_FT_FI2
Number of Residues3
DetailsSITE: Cleavage
ChainResidueDetails
AASP208
AASP216
AASP251

site_idSWS_FT_FI3
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER289
ASER291
ASER302

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079
ChainResidueDetails
ASER645
ASER666

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by RIOK3 => ECO:0000250|UniProtKB:Q9BYX4
ChainResidueDetails
AVAL846

site_idSWS_FT_FI6
Number of Residues3
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ISG15) => ECO:0000250|UniProtKB:Q9BYX4
ChainResidueDetails
ALYS23
ALYS43

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PDB entries from 2024-05-01

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