9Q5W: Human MDA5 T331I mutant

CryoEM Structure of human MDA5 T331I mutant in complex with dsRNA. Determined by electron microscopy at 3.21 Å resolution. Released 16 Sept 2026.

Method
Electron microscopy
Resolution
3.21 Å
Organisms
Homo sapiens, synthetic construct
Chains
4
Atoms
12,241
Mol. weight
186.97 kDa
Ligands
ATP
Released
16 Sept 2026

Explore 9Q5W in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9Q5W contains 62 α-helices and 54 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain C: 30 helices, 28 β-strands

ElementResiduesLengthSheet
α-helix310-32011
β-strand325-32841
α-helix335-35218
β-strand359-36351
α-helix366-3727
α-helix373-3775
α-helix378-3803
β-strand387-39041
α-helix395-3973
α-helix400-4067
β-strand409-41351
α-helix414-42613
β-strand439-44351
α-helix445-4473
α-helix453-47321
β-strand483-48861
α-helix499-51214
β-strand517-51931
α-helix525-5317
α-helix5351
β-strand536-53942
β-strand54213
α-helix549-56517
α-helix5721
α-helix576-59217
α-helix595-61622
α-helix619-64022
α-helix671-69121
α-helix699-71214
β-strand721-72552
α-helix728-74013
α-helix742-7476
β-strand751-75442
α-helix764-7674
α-helix768-78013
β-strand787-79042
β-strand79414
β-strand79614
β-strand803-80752
α-helix813-8208
β-strand829-83352
β-strand83513
α-helix840-86223
α-helix866-89025
α-helix900-9023
β-strand903-90755
β-strand913-91645
β-strand921-92336
β-strand927-92936
α-helix933-9386
β-strand940-94126
β-strand959-96136
β-strand967-97486
β-strand977-98266
β-strand987-99155
β-strand996-99945
α-helix1003-10053
β-strand101216
Chain I: 32 helices, 26 β-strands
ElementResiduesLengthSheet
α-helix310-32011
β-strand325-32847
α-helix335-35218
β-strand359-36357
α-helix366-3727
α-helix373-3775
α-helix378-3803
β-strand387-39047
α-helix395-3973
α-helix400-4045
β-strand409-41357
α-helix414-42613
β-strand439-44357
α-helix445-4473
α-helix453-47321
α-helix476-4827
β-strand483-48867
α-helix499-51214
β-strand517-51937
α-helix525-5317
α-helix533-5353
β-strand536-54278
α-helix549-56416
α-helix5721
α-helix576-59217
α-helix595-61622
α-helix620-64122
α-helix671-69222
α-helix699-71315
β-strand721-72558
α-helix728-74013
α-helix742-7476
β-strand751-75448
α-helix764-7674
α-helix768-77912
β-strand787-79048
β-strand803-80758
α-helix813-82210
β-strand829-83578
α-helix840-86223
α-helix866-89025
α-helix900-9023
β-strand903-90759
β-strand913-91649
β-strand920-923410
β-strand927-930410
α-helix933-9386
β-strand940-942311
α-helix9581
β-strand959-961311
β-strand970111
β-strand971-974412
β-strand977-980412
β-strand981110
α-helix984-9863
β-strand987-99159
β-strand99819
β-strand1012110

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Interferon-induced helicase C domain-containing protein 1C, Iprotein728Homo sapiensQ9BYX4 (AlphaFold model)
RNA (29-mer)BRNA29synthetic construct
RNA (29-mer)ARNA29synthetic construct
Sequence of entity 1 (C, I), FASTA
>9Q5W_1 Interferon-induced helicase C domain-containing protein 1 (chains C, I)
ARASPEPELQLRPYQMEVAQPALEGKNIIICLPIGSGKTRVAVYIAKDHLDKKKKASEPG
KVIVLVNKVLLVEQLFRKEFQPFLKKWYRVIGLSGDTQLKISFPEVVKSCDIIISTAQIL
ENSLLNLENGEDAGVQLSDFSLIIIDECHHTNKEAVYNNIMRHYLMQKLKNNRLKKENKP
VIPLPQILGLTASPGVGGATKQAKAEEHILKLCANLDAFTIKTVKENLDQLKNQIQEPCK
KFAIADATREDPFKEKLLEIMTRIQTYCQMSPMSDFGTQPYEQWAIQMEKKAAKEGNRKE
RVCAEHLRKYNEALQINDTIRMIDAYTHLETFYNEEKDKKFAVIEDDSDEGGDDEYCDGD
EDEDDLKKPLKLDETDRFLMTLFFENNKMLKRLAENPEYENEKLTKLRNTIMEQYTRTEE
SARGIIFTKTRQSAYALSQWITENEKFAEVGVKAHHLIGAGHSSEFKPMTQNEQKEVISK
FRTGKINLLIATTVAEEGLDIKECNIVIRYGLVTNEIAMVQARGRARADESTYVLVAHSG
SGVIEHETVNDFREKMMYKAIHCVQNMKPEEYAHKILELQMQSIMEKKMKTKRNIAKHYK
NNPSLITFLCKNCSVLACSGEDIHVIEKMHHVNMTPEFKELYIVRENKALQKKCADYQIN
GEIICKCGQAWGTMMVHKGLDLPCLKIRNFVVVFKNNSTKKQYKKWVELPITFPNLDYSE
CCLFSDED
Sequence of entity 2 (B), FASTA
>9Q5W_2 RNA (29-MER) (chains B)
UUCGGUUAGGGGCUAGGACGAUAUUAUUG
Sequence of entity 3 (A), FASTA
>9Q5W_3 RNA (29-MER) (chains A)
CAAUAAUAUCGUCCUAGCCCCUAACCGAA

Ligands and cofactors

IDNameFormulaCopies
ATPAdenosine-5'-triphosphateC10 H16 N5 O13 P32

Primary citation

Unraveling the molecular basis for MDA5 T331I disease-linked mutation. Xu, L., Chung, K., Guo, R. et al. To be published.

Other PDB entries of the same protein (UniProt Q9BYX4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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