6WJ5: Human TRPA1

Structure of human TRPA1 in complex with inhibitor GDC-0334. Determined by electron microscopy at 3.6 Å resolution. Released 17 Feb 2021.

Method: Electron microscopy
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 4
Atoms: 18,052
Mol. weight: 292.93 kDa
Ligands: LXY
Released: 17 Feb 2021

Explore 6WJ5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 36 helices, 6 β-strands

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

Chain B: 34 helices, 8 β-strands

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

Chain C: 35 helices, 8 β-strands

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

Chain D: 36 helices, 10 β-strands

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

Molecules and chains

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)

Sequence of entity 1 (A, B, C, D), FASTA

>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

Ligands and cofactors

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

Primary citation

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:

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,…
9MOE 2.7 Å, Preclinical and clinical evaluation of a novel TRPA1 antagonist LY3526318
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

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