9M8S: Human TRPA1 ion channel in ligand-free state

Cryo-EM structure of the human TRPA1 ion channel in ligand-free state. Determined by electron microscopy at 3.1 Å resolution. Released 29 Oct 2025.

Method
Electron microscopy
Resolution
3.1 Å
Organism
Homo sapiens
Chains
4
Atoms
18,304
Mol. weight
510.64 kDa
Released
29 Oct 2025

Explore 9M8S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9M8S contains 140 α-helices and 16 β-strands across 4 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.

Chains A, B, C and D: 35 helices, 4 β-strands

ElementResiduesLengthSheet
α-helix448-4558
α-helix459-4668
α-helix485-4928
α-helix495-5039
α-helix512-5143
α-helix517-5248
α-helix527-5348
α-helix551-5588
α-helix561-5699
α-helix583-5897
α-helix593-6019
α-helix605-6106
α-helix622-6298
α-helix631-64010
β-strand657-65933
α-helix684-6918
α-helix695-6984
α-helix701-71010
α-helix711-7155
α-helix716-73924
β-strand74614
β-strand75114
α-helix767-78923
α-helix803-81816
α-helix820-8223
α-helix828-84922
α-helix857-89135
α-helix896-8983
α-helix901-91111
α-helix9181
α-helix919-9235
α-helix924-9274
α-helix934-94512
α-helix946-9527
α-helix953-96917
α-helix971-98919
α-helix993-9986
β-strand1002-100433
α-helix1041-107131

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transient receptor potential cation channel subfamily A member 1A, B, C, Dprotein1119Homo sapiensO75762 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>9M8S_1 Transient receptor potential cation channel subfamily A member 1 (chains A, B, C, D)
MKRSLRKMWRPGEKKEPQGVVYEDVPDDTEDFKESLKVVFEGSAYGLQNFNKQKKLKRCD
DMDTFFLHYAAAEGQIELMEKITRDSSLEVLHEMDDYGNTPLHCAVEKNQIESVKFLLSR
GANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSEA
LQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGEEHGYSRQLHINFMNNGKA
TPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSYSGSVD
IVNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNL
LLSKGAQVDIKDNFGRNFLHLTVQQPYGLKNLRPEFMQMQQIKELVMDEDNDGCTPLHYA
CRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTRLLNEGDL
HGMTPLHLAAKNGHDKVVQLLLKKGALFLSDHNGWTALHHASMGGYTQTMKVILDTNLKC
TDRLDEDGNTALHFAAREGHAKAVALLLSHNADIVLNKQQASFLHLALHNKRKEVVLTII
RSKRWDECLKIFSHNSPGNKCPITEMIEYLPECMKVLLDFCMLHSTEDKSCRDYYIEYNF
KYLQCPLEFTKKTPTQDVIYEPLTALNAMVQNNRIELLNHPVCKEYLLMKWLAYGFRAHM
MNLGSYCLGLIPMTILVVNIKPGMAFNSTGIINETSDHSEILDTTNSYLIKTCMILVFLS
SIFGYCKEAGQIFQQKRNYFMDISNVLEWIIYTTGIIFVLPLFVEIPAHLQWQCGAIAVY
FYWMNFLLYLQRFENCGIFIVMLEVILKTLLRSTVVFIFLLLAFGLSFYILLNLQDPFSS
PLLSIIQTFSMMLGDINYRESFLEPYLRNELAHPVLSFAQLVSFTIFVPIVLMNLLIGLA
VGDIAEVQKHASLKRIAMQVELHTSLEKKLPLWFLRKVDQKSTIVYPNKPRSGGMLFHIF
CFLFCTGEIRQEIPNADKSLEMEILKQKYRLKDLTFLLEKQHELIKLIIQKMEIISETED
DDSHCSFQDRFKKEQMEQRNSRWNTVLRAVKAKTHHLEP

Primary citation

Binding and Activating of Analgesic Crotalphine with Human TRPA1. Kang, M., Zhang, Y., Ding, X. et al. Membranes (Basel) (2025) 15. DOI 10.3390/membranes15060187 · PubMed

Other PDB entries of the same protein (UniProt O75762 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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