Structure of human TRPA1 in complex with inhibitor GDC-0334. Determined by electron microscopy at 3.6 Å resolution. Released 17 Feb 2021.
Explore 6WJ5 in 3D Show helices and sheets RCSB PDB PDBe
6WJ5 contains 141 α-helices and 32 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 | 459-465 | 7 | |
| α-helix | 485-492 | 8 | |
| α-helix | 495-504 | 10 | |
| α-helix | 517-523 | 7 | |
| α-helix | 527-537 | 11 | |
| 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 | 605-608 | 4 | |
| α-helix | 622-629 | 8 | |
| α-helix | 631-640 | 10 | |
| 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 | 750-752 | 3 | 2 |
| β-strand | 762-763 | 2 | 2 |
| α-helix | 767-787 | 21 | |
| α-helix | 804-815 | 12 | |
| 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 | 901-910 | 10 | |
| α-helix | 911-913 | 3 | |
| α-helix | 918 | 1 | |
| α-helix | 919-923 | 5 | |
| α-helix | 924-926 | 3 | |
| α-helix | 934-946 | 13 | |
| α-helix | 947-952 | 6 | |
| α-helix | 953-987 | 35 | |
| α-helix | 992-998 | 7 | |
| β-strand | 1002-1005 | 4 | 1 |
| 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 | 495-504 | 10 | |
| α-helix | 517-524 | 8 | |
| α-helix | 527-537 | 11 | |
| α-helix | 551-557 | 7 | |
| α-helix | 561-569 | 9 | |
| β-strand | 577 | 1 | 3 |
| β-strand | 581 | 1 | 3 |
| α-helix | 583-588 | 6 | |
| α-helix | 593-601 | 9 | |
| α-helix | 605-608 | 4 | |
| α-helix | 622-629 | 8 | |
| α-helix | 631-640 | 10 | |
| β-strand | 642-644 | 3 | 4 |
| β-strand | 656-659 | 4 | 4 |
| 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 | 5 |
| β-strand | 750-752 | 3 | 5 |
| β-strand | 762-763 | 2 | 5 |
| α-helix | 767-787 | 21 | |
| α-helix | 804-815 | 12 | |
| α-helix | 820-822 | 3 | |
| α-helix | 828-844 | 17 | |
| α-helix | 847-850 | 4 | |
| α-helix | 854-891 | 38 | |
| α-helix | 896-898 | 3 | |
| α-helix | 901-911 | 11 | |
| α-helix | 918 | 1 | |
| α-helix | 919-923 | 5 | |
| α-helix | 924-926 | 3 | |
| α-helix | 934-946 | 13 | |
| α-helix | 947-952 | 6 | |
| α-helix | 953-989 | 37 | |
| α-helix | 992-998 | 7 | |
| β-strand | 1002-1005 | 4 | 4 |
| 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 | 495-504 | 10 | |
| α-helix | 517-523 | 7 | |
| α-helix | 527-533 | 7 | |
| α-helix | 538-540 | 3 | |
| α-helix | 551-557 | 7 | |
| α-helix | 561-569 | 9 | |
| β-strand | 577 | 1 | 6 |
| β-strand | 581 | 1 | 6 |
| α-helix | 583-588 | 6 | |
| α-helix | 593-601 | 9 | |
| α-helix | 605-608 | 4 | |
| α-helix | 622-629 | 8 | |
| α-helix | 631-640 | 10 | |
| 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 | 746-747 | 2 | 8 |
| β-strand | 750-752 | 3 | 8 |
| β-strand | 762-763 | 2 | 8 |
| α-helix | 767-787 | 21 | |
| α-helix | 804-815 | 12 | |
| α-helix | 820-822 | 3 | |
| α-helix | 828-850 | 23 | |
| 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 | 924-926 | 3 | |
| α-helix | 934-946 | 13 | |
| α-helix | 947-952 | 6 | |
| α-helix | 953-967 | 15 | |
| α-helix | 971-989 | 19 | |
| α-helix | 992-998 | 7 | |
| β-strand | 1002-1005 | 4 | 7 |
| α-helix | 1040-1071 | 32 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 449-455 | 7 | |
| α-helix | 459-465 | 7 | |
| α-helix | 485-491 | 7 | |
| α-helix | 495-504 | 10 | |
| α-helix | 517-523 | 7 | |
| α-helix | 527-534 | 8 | |
| α-helix | 538-542 | 5 | |
| β-strand | 544 | 1 | 9 |
| β-strand | 550 | 1 | 9 |
| α-helix | 551-557 | 7 | |
| α-helix | 561-569 | 9 | |
| β-strand | 577 | 1 | 10 |
| β-strand | 581 | 1 | 10 |
| 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 | 11 |
| β-strand | 656-659 | 4 | 11 |
| 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 | 12 |
| β-strand | 750-752 | 3 | 12 |
| β-strand | 762-763 | 2 | 12 |
| α-helix | 767-787 | 21 | |
| α-helix | 804-815 | 12 | |
| 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 | 901-910 | 10 | |
| α-helix | 911-913 | 3 | |
| α-helix | 918 | 1 | |
| α-helix | 919-923 | 5 | |
| α-helix | 924-926 | 3 | |
| 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 | 11 |
| 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) |
>6WJ5_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 |
|---|---|---|---|
| LXY | (4R,5S)-4-fluoro-1-[(4-fluorophenyl)sulfonyl]-5-methyl-N-({5-(trifluoromethyl)-… | C24 H19 F8 N5 O3 S | 4 |
A TRPA1 inhibitor suppresses neurogenic inflammation and airway contraction for asthma treatment. Balestrini, A., Joseph, V., Dourado, M. et al. J Exp Med (2021) 218. DOI 10.1084/jem.20201637 · 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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