9MOE: PDB entry 9MOE

Preclinical and clinical evaluation of a novel TRPA1 antagonist LY3526318. Determined by electron microscopy at 2.7 Å resolution. Released 21 May 2025.

Method

Electron microscopy

Resolution

2.7 Å

Organism

Homo sapiens

Chains

4

Atoms

17,591

Mol. weight

513.02 kDa

Ligands

A1BNO

Released

21 May 2025

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

Secondary structure: helices and β-sheets

9MOE contains 144 α-helices and 24 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.

Chain A: 36 helices, 6 β-strands

Molecules and chains

>9MOE_1 Transient receptor potential cation channel subfamily A member 1 (chains A, B, D, E)
LGKRSLRKMWRPGEKKEPQGVVYEDVPDDTEDFKESLKVVFEGSAYGLQNFNKQKKLKRC
DDMDTFFLHYAAAEGQIELMEKITRDSSLEVLHEMDDYGNTPLHCAVEKNQIESVKFLLS
RGANPNLRNFNMMAPLHIAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSE
ALQILLKKGAKPCKSNKWGCFPIHQAAFSGSKECMEIILRFGEEHGYSRQLHINFMNNGK
ATPLHLAVQNGDLEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSYSGSV
DIVNTTDGCHETMLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVN
LLLSKGAQVDIKDNFGRNFLHLTVQQPYGLKNLRPEFMQMQQIKELVMDEDNDGCTPLHY
ACRQGGPGSVNNLLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTRLLNEGD
LHGMTPLHLAAKNGHDKVVQLLLKKGALFLSDHNGWTALHHASMGGYTQTMKVILDTNLK
CTDRLDEDGNTALHFAAREGHAKAVALLLSHNADIVLNKQQASFLHLALHNKRKEVVLTI
IRSKRWDECLKIFSHNSPGNKCPITEMIEYLPECMKVLLDFCMLHSTEDKSCRDYYIEYN
FKYLQCPLEFTKKTPTQDVIYEPLTALNAMVQNNRIELLNHPVCKEYLLMKWLAYGFRAH
MMNLGSYCLGLIPMTILVVNIKPGMAFNSTGIINETSDHSEILDTTNSYLIKTCMILVFL
SSIFGYCKEAGQIFQQKRNYFMDISNVLEWIIYTTGIIFVLPLFVEIPAHLQWQCGAIAV
YFYWMNFLLYLQRFENCGIFIVMLEVILKTLLRSTVVFIFLLLAFGLSFYILLNLQDPFS
SPLLSIIQTFSMMLGDINYRESFLEPYLRNELAHPVLSFAQLVSFTIFVPIVLMNLLIGL
AVGDIAEVQKHASLKRIAMQVELHTSLEKKLPLWFLRKVDQKSTIVYPNKPRSGGMLFHI
FCFLFCTGEIRQEIPNADKSLEMEILKQKYRLKDLTFLLEKQHELIKLIIQKMEIISETE
DDDSHCSFQDRFKKEQMEQRNSRWNTVLRAVKAKTHHLEP

Ligands and cofactors

Primary citation

Preclinical and clinical evaluation of a novel TRPA1 antagonist LY3526318. Broad, L.M., Suico, J.G., Turner, P.K. et al. Pain (2025) 166:1893-1908. DOI 10.1097/j.pain.0000000000003570 · PubMed

Related structures

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

• 6HC8 1.9 Å, Factor Inhibiting HIF (FIH) in complex with zinc, NOG and TRPA1 (313-339)
• 9VU1 2.59 Å, Structure of hTRPA1 complexed with LIQA
• 6V9V 2.6 Å, Structure of TRPA1 modified by Bodipy-iodoacetamide with bound calcium, LMNG
• 7OR0 2.64 Å, Cryo-EM structure of the human TRPA1 ion channel in complex with the antagonist 3-60,…
• 7OR1 2.64 Å, Cryo-EM structure of the human TRPA1 ion channel in complex with the antagonist 3-60,…
• 6PQQ 2.81 Å, Cryo-EM structure of human TRPA1 C621S mutant in the apo state
• 6PQO 2.88 Å, Cryo-EM structure of the human TRPA1 ion channel in complex with the covalent agonist…
• 6X2J 3.0 Å, Structure of human TRPA1 in complex with agonist GNE551
• 7JUP 3.05 Å, Structure of human TRPA1 in complex with antagonist compound 21
• 6PQP 3.06 Å, Cryo-EM structure of the human TRPA1 ion channel in complex with the covalent agonist BITC
• 6V9W 3.1 Å, Structure of TRPA1 (ligand-free) with bound calcium, LMNG
• 9M8S 3.1 Å, Cryo-EM structure of the human TRPA1 ion channel in ligand-free state.

Browse structure collections

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