Structure of the TRPA1 ion channel determined by electron cryo-microscopy. Determined by electron microscopy at 4.24 Å resolution. Released 8 Apr 2015.
Explore 3J9P in 3D Show helices and sheets RCSB PDB PDBe
3J9P contains 108 α-helices and 0 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 | 449-456 | 8 | |
| α-helix | 459-466 | 8 | |
| α-helix | 482 | 1 | |
| α-helix | 485-491 | 7 | |
| α-helix | 495-504 | 10 | |
| α-helix | 517-521 | 5 | |
| α-helix | 528-536 | 9 | |
| α-helix | 551-555 | 5 | |
| α-helix | 561-568 | 8 | |
| α-helix | 583-588 | 6 | |
| α-helix | 593-601 | 9 | |
| α-helix | 621-626 | 6 | |
| α-helix | 630-636 | 7 | |
| α-helix | 685-690 | 6 | |
| α-helix | 701-705 | 5 | |
| α-helix | 706-739 | 34 | |
| α-helix | 767-782 | 16 | |
| α-helix | 804-819 | 16 | |
| α-helix | 820-822 | 3 | |
| α-helix | 829-849 | 21 | |
| α-helix | 859-891 | 33 | |
| α-helix | 901-912 | 12 | |
| α-helix | 923-928 | 6 | |
| α-helix | 934-947 | 14 | |
| α-helix | 951-969 | 19 | |
| α-helix | 971-987 | 17 | |
| α-helix | 1041-1070 | 30 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Maltose-binding periplasmic protein, Transient receptor potential cation channel subfamily A… | A, B, C, D | protein | 1528 | Escherichia coli, Homo sapiens | O75762 (AlphaFold model), P0AEX9 (AlphaFold model) |
>3J9P_1 Maltose-binding periplasmic protein, Transient receptor potential cation channel subfamily A member 1 chimera (chains A, B, C, D) MGSSHHHHHHHHGSSMKIEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLE EKFPQVAATGDGPDIIFWAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLI AYPIAVEALSLIYNKDLLPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAAD GGYAFKYENGKYDIKDVGVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAM TINGPWAWSNIDTSKVNYGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYL LTDEGLEAVNKDKPLGAVALKSYEEELAKDPRIAATMENAQKGEIMPNIPQMSAFWYAVR TAVINAASGRQTVDEALKDAQTNSSSNNNNNNNNNNLGIEENLYFQGAGSKRSLRKMWRP GEKKEPQGVVYEDVPDDTEDFKESLKVVFEGSAYGLQNFNKQKKLKRCDDMDTFFLHYAA AEGQIELMEKITRDSSLEVLHEMDDYGNTPLHCAVEKNQIESVKFLLSRGANPNLRNFNM MAPLHIAVQGMNNEVMKVLLEHRTIDVNLEGENGNTAVIIACTTNNSEALQILLKKGAKP CKSNKWGCFPIHQAAFSGSKECMEIILRFGEEHGYSRQLHINFMNNGKATPLHLAVQNGD LEMIKMCLDNGAQIDPVEKGRCTAIHFAATQGATEIVKLMISSYSGSVDIVNTTDGCHET MLHRASLFDHHELADYLISVGADINKIDSEGRSPLILATASASWNIVNLLLSKGAQVDIK DNFGRNFLHLTVQQPYGLKNLRPEFMQMQQIKELVMDEDNDGCTPLHYACRQGGPGSVNN LLGFNVSIHSKSKDKKSPLHFAASYGRINTCQRLLQDISDTRLLNEGDLHGMTPLHLAAK NGHDKVVQLLLKKGALFLSDHNGWTALHHASMGGYTQTMKVILDTNLKCTDRLDEDGNTA LHFAAREGHAKAVALLLSHNADIVLNKQQASFLHLALHNKRKEVVLTIIRSKRWDECLKI FSHNSPGNKCPITEMIEYLPECMKVLLDFCMLHSTEDKSCRDYYIEYNFKYLQCPLEFTK KTPTQDVIYEPLTALNAMVQNNRIELLNHPVCKEYLLMKWLAYGFRAHMMNLGSYCLGLI PMTILVVNIKPGMAFNSTGIINETSDHSEILDTTNSYLIKTCMILVFLSSIFGYCKEAGQ IFQQKRNYFMDISNVLEWIIYTTGIIFVLPLFVEIPAHLQWQCGAIAVYFYWMNFLLYLQ RFENCGIFIVMLEVILKTLLRSTVVFIFLLLAFGLSFYILLNLQDPFSSPLLSIIQTFSM MLGDINYRESFLEPYLRNELAHPVLSFAQLVSFTIFVPIVLMNLLIGLAVGDIADVQKHA SLKRIAMQVELHTSLEKKLPLWFLRKVDQKSTIVYPNKPRSGGMLFHIFCFLFCTGEIRQ EIPNADKSLEMEILKQKYRLKDLTFLLEKQHELIKLIIQKMEIISETEDDDSHCSFQDRF KKEQMEQRNSRWNTVLRAVKAKTHHLEP
Structure of the TRPA1 ion channel suggests regulatory mechanisms. Paulsen, C.E., Armache, J.-P., Gao, Y. et al. Nature (2015) 520:511-517. DOI 10.1038/nature14367 · 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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