Structure of human TRPA1 in complex with antagonist compound 21. Determined by electron microscopy at 3.05 Å resolution. Released 31 Mar 2021.
Explore 7JUP in 3D Show helices and sheets RCSB PDB PDBe
7JUP contains 142 α-helices and 20 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 449-455 | 7 | |
| α-helix | 459-468 | 10 | |
| α-helix | 472-475 | 4 | |
| α-helix | 477-479 | 3 | |
| α-helix | 485-492 | 8 | |
| α-helix | 495-503 | 9 | |
| α-helix | 517-523 | 7 | |
| α-helix | 527-536 | 10 | |
| α-helix | 538-540 | 3 | |
| α-helix | 551-557 | 7 | |
| α-helix | 561-569 | 9 | |
| α-helix | 583-588 | 6 | |
| α-helix | 593-601 | 9 | |
| α-helix | 605-610 | 6 | |
| α-helix | 622-629 | 8 | |
| α-helix | 631-639 | 9 | |
| β-strand | 642-644 | 3 | 1 |
| β-strand | 656-659 | 4 | 1 |
| α-helix | 684-691 | 8 | |
| α-helix | 695-698 | 4 | |
| α-helix | 701-710 | 10 | |
| α-helix | 711-715 | 5 | |
| α-helix | 716-738 | 23 | |
| β-strand | 746-747 | 2 | 2 |
| β-strand | 750-751 | 2 | 2 |
| α-helix | 767-787 | 21 | |
| α-helix | 804-817 | 14 | |
| α-helix | 820-822 | 3 | |
| α-helix | 828-844 | 17 | |
| α-helix | 847-852 | 6 | |
| α-helix | 857-891 | 35 | |
| α-helix | 896-898 | 3 | |
| α-helix | 901-911 | 11 | |
| α-helix | 918 | 1 | |
| α-helix | 919-923 | 5 | |
| α-helix | 924-927 | 4 | |
| α-helix | 934-945 | 12 | |
| α-helix | 946-952 | 7 | |
| α-helix | 953-989 | 37 | |
| α-helix | 992-998 | 7 | |
| β-strand | 1002-1005 | 4 | 1 |
| α-helix | 1040-1043 | 4 | |
| α-helix | 1045-1071 | 27 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 449-455 | 7 | |
| α-helix | 459-468 | 10 | |
| α-helix | 485-492 | 8 | |
| α-helix | 495-503 | 9 | |
| α-helix | 517-523 | 7 | |
| α-helix | 527-536 | 10 | |
| α-helix | 551-558 | 8 | |
| α-helix | 561-569 | 9 | |
| α-helix | 583-588 | 6 | |
| α-helix | 593-600 | 8 | |
| α-helix | 605-608 | 4 | |
| α-helix | 622-629 | 8 | |
| α-helix | 631-639 | 9 | |
| β-strand | 642-644 | 3 | 3 |
| β-strand | 656-659 | 4 | 3 |
| α-helix | 684-691 | 8 | |
| α-helix | 695-698 | 4 | |
| α-helix | 701-710 | 10 | |
| α-helix | 711-715 | 5 | |
| α-helix | 716-739 | 24 | |
| β-strand | 746-747 | 2 | 4 |
| β-strand | 750-751 | 2 | 4 |
| α-helix | 767-787 | 21 | |
| α-helix | 804-819 | 16 | |
| α-helix | 820-822 | 3 | |
| α-helix | 828-844 | 17 | |
| α-helix | 848-852 | 5 | |
| α-helix | 857-891 | 35 | |
| α-helix | 896-898 | 3 | |
| α-helix | 901-911 | 11 | |
| α-helix | 918 | 1 | |
| α-helix | 919-923 | 5 | |
| α-helix | 924-927 | 4 | |
| α-helix | 934-945 | 12 | |
| α-helix | 946-952 | 7 | |
| α-helix | 953-989 | 37 | |
| α-helix | 992-998 | 7 | |
| β-strand | 1002-1005 | 4 | 3 |
| α-helix | 1040-1071 | 32 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 449-455 | 7 | |
| α-helix | 459-465 | 7 | |
| α-helix | 485-492 | 8 | |
| α-helix | 495-503 | 9 | |
| α-helix | 517-523 | 7 | |
| α-helix | 527-536 | 10 | |
| α-helix | 539-542 | 4 | |
| α-helix | 551-558 | 8 | |
| α-helix | 561-569 | 9 | |
| α-helix | 583-588 | 6 | |
| α-helix | 593-601 | 9 | |
| α-helix | 605-608 | 4 | |
| α-helix | 622-629 | 8 | |
| α-helix | 631-639 | 9 | |
| β-strand | 642-644 | 3 | 5 |
| β-strand | 656-659 | 4 | 5 |
| α-helix | 684-691 | 8 | |
| α-helix | 695-698 | 4 | |
| α-helix | 701-710 | 10 | |
| α-helix | 711-715 | 5 | |
| α-helix | 716-738 | 23 | |
| β-strand | 746-747 | 2 | 6 |
| β-strand | 750-751 | 2 | 6 |
| α-helix | 767-787 | 21 | |
| α-helix | 804-817 | 14 | |
| α-helix | 820-822 | 3 | |
| α-helix | 828-844 | 17 | |
| α-helix | 847-850 | 4 | |
| α-helix | 857-891 | 35 | |
| α-helix | 896-898 | 3 | |
| α-helix | 901-911 | 11 | |
| α-helix | 918 | 1 | |
| α-helix | 919-923 | 5 | |
| α-helix | 924-927 | 4 | |
| α-helix | 934-945 | 12 | |
| α-helix | 946-952 | 7 | |
| α-helix | 953-989 | 37 | |
| α-helix | 992-998 | 7 | |
| β-strand | 1002-1005 | 4 | 5 |
| α-helix | 1040-1071 | 32 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 449-455 | 7 | |
| α-helix | 459-468 | 10 | |
| α-helix | 485-492 | 8 | |
| α-helix | 495-503 | 9 | |
| α-helix | 517-523 | 7 | |
| α-helix | 527-534 | 8 | |
| α-helix | 538-542 | 5 | |
| α-helix | 551-558 | 8 | |
| α-helix | 561-569 | 9 | |
| α-helix | 583-588 | 6 | |
| α-helix | 593-600 | 8 | |
| α-helix | 605-608 | 4 | |
| α-helix | 622-629 | 8 | |
| α-helix | 631-639 | 9 | |
| β-strand | 642-644 | 3 | 7 |
| β-strand | 656-659 | 4 | 7 |
| α-helix | 684-691 | 8 | |
| α-helix | 695-698 | 4 | |
| α-helix | 701-710 | 10 | |
| α-helix | 711-715 | 5 | |
| α-helix | 716-738 | 23 | |
| β-strand | 745-747 | 3 | 8 |
| β-strand | 750-752 | 3 | 8 |
| α-helix | 767-787 | 21 | |
| α-helix | 804-819 | 16 | |
| α-helix | 820-822 | 3 | |
| α-helix | 828-846 | 19 | |
| α-helix | 848-850 | 3 | |
| α-helix | 857-891 | 35 | |
| α-helix | 896-898 | 3 | |
| α-helix | 901-911 | 11 | |
| α-helix | 918 | 1 | |
| α-helix | 919-923 | 5 | |
| α-helix | 924-927 | 4 | |
| α-helix | 934-945 | 12 | |
| α-helix | 946-952 | 7 | |
| α-helix | 953-989 | 37 | |
| α-helix | 992-998 | 7 | |
| β-strand | 1002-1005 | 4 | 7 |
| α-helix | 1040-1071 | 32 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transient receptor potential cation channel subfamily A member 1 | A, B, C, D | protein | 631 | Homo sapiens | O75762 (AlphaFold model) |
>7JUP_1 Transient receptor potential cation channel subfamily A member 1 (chains A, B, C, D) SPLHFAASYGRINTCQRLLQDISDTRLLNEGDLHGMTPLHLAAKNGHDKVVQLLLKKGAL FLSDHNGWTALHHASMGGYTQTMKVILDTNLKCTDRLDEDGNTALHFAAREGHAKAVALL LSHNADIVLNKQQASFLHLALHNKRKEVVLTIIRSKRWDECLKIFSHNSPGNKCPITEMI EYLPECMKVLLDFCMLHSTEDKSCRDYYIEYNFKYLQCPLEFTKKTPTQDVIYEPLTALN AMVQNNRIELLNHPVCKEYLLMKWLAYGFRAHMMNLGSYCLGLIPMTILVVNIKPGMAFN STGIINETSDHSEILDTTNSYLIKTCMILVFLSSIFGYCKEAGQIFQQKRNYFMDISNVL EWIIYTTGIIFVLPLFVEIPAHLQWQCGAIAVYFYWMNFLLYLQRFENCGIFIVMLEVIL KTLLRSTVVFIFLLLAFGLSFYILLNLQDPFSSPLLSIIQTFSMMLGDINYRESFLEPYL RNELAHPVLSFAQLVSFTIFVPIVLMNLLIGLAVGDIADVQKHASLKRIAMQVELHTSLE KKLPLWFLRKVDQKSTIVYPNKPRSGGMLFHIFCFLFCTGEIRQEIPNADKSLEMEILKQ KYRLKDLTFLLEKQHELIKLIIQKMEIISET
| ID | Name | Formula | Copies |
|---|---|---|---|
| VKM | 1-({3-[(3R,5R)-5-(4-fluorophenyl)oxolan-3-yl]-1,2,4-oxadiazol-5-yl}methyl)-7-me… | C19 H17 F N6 O3 | 4 |
Tetrahydrofuran-Based Transient Receptor Potential Ankyrin 1 (TRPA1) Antagonists: Ligand-Based Discovery, Activity in a Rodent Asthma Model, and Mechanism-of-Action via Cryogenic Electron Microscopy. Terrett, J.A., Chen, H., Shore, D.G. et al. J Med Chem (2021) 64:3843-3869. DOI 10.1021/acs.jmedchem.0c02023 · 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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