7DXE: TRPC3 gain of function mutation R803C

Structure of TRPC3 gain of function mutation R803C at 3.2 angstrom in 1340nM free calcium state. Determined by electron microscopy at 3.2 Å resolution. Released 2 Feb 2022.

Method: Electron microscopy
Resolution: 3.2 Å
Organism: Homo sapiens
Chains: 4
Atoms: 22,280
Mol. weight: 394.15 kDa
Ligands: 98R, POV, ZN, Y01
Released: 2 Feb 2022

Explore 7DXE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7DXE contains 160 α-helices and 16 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.

Chains A, B, C and D: 40 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	26-37	12
α-helix	40-47	8
α-helix	65-71	7
α-helix	75-82	8
α-helix	90-99	10
α-helix	103-110	8
α-helix	113-116	4
β-strand	137	1	3
β-strand	143	1	3
α-helix	151-158	8
α-helix	161-169	9
α-helix	174-179	6
α-helix	185-192	8
α-helix	195-209	15
α-helix	212-218	7
α-helix	222-240	19
α-helix	244-263	20
α-helix	268-275	8
α-helix	295-302	8
α-helix	306-309	4
α-helix	312-322	11
α-helix	328-330	3
α-helix	334-354	21
α-helix	358-360	3
α-helix	362-368	7
α-helix	370-391	22
α-helix	415-420	6
α-helix	421-423	3
α-helix	424-447	24
α-helix	449-454	6
α-helix	456-492	37
α-helix	505-508	4
α-helix	509-511	3
α-helix	522-537	16
α-helix	538-543	6
α-helix	545-547	3
α-helix	552-587	36
α-helix	588-590	3
β-strand	594	1	4
α-helix	602-611	10
β-strand	624	1	4
α-helix	629-661	33
α-helix	668-685	18
α-helix	762-784	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Short transient receptor potential channel 3	A, B, C, D	protein	836	Homo sapiens	Q13507 (AlphaFold model)

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

>7DXE_1 Short transient receptor potential channel 3 (chains A, B, C, D)
MREKGRRQAVRGPAFMFNDRGTSLTAEEERFLDAAEYGNIPVVRKMLEESKTLNVNCVDY
MGQNALQLAVGNEHLEVTELLLKKENLARIGDALLLAISKGYVRIVEAILNHPGFAASKR
LTLSPCEQELQDDDFYAYDEDGTRFSPDITPIILAAHCQKYEVVHMLLMKGARIERPHDY
FCKCGDCMEKQRHDSFSHSRSRINAYKGLASPAYLSLSSEDPVLTALELSNELAKLANIE
KEFKNDYRKLSMQCKDFVVGVLDLCRDSEEVEAILNGDLESAEPLEVHRHKASLSRVKLA
IKYEVKKFVAHPNCQQQLLTIWYENLSGLREQTIAIKCLVVLVVALGLPFLAIGYWIAPC
SRLGKILRSPFMKFVAHAASFIIFLGLLVFNASDRFEGITTLPNITVTDYPKQIFRVKTT
QFTWTEMLIMVWVLGMMWSECKELWLEGPREYILQLWNVLDFGMLSIFIAAFTARFLAFL
QATKAQQYVDSYVQESDLSEVTLPPEIQYFTYARDKWLPSDPQIISEGLYAIAVVLSFSR
IAYILPANESFGPLQISLGRTVKDIFKFMVLFIMVFFAFMIGMFILYSYYLGAKVNAAFT
TVEESFKTLFWSIFGLSEVTSVVLKYDHKFIENIGYVLYGIYNVTMVVVLLNMLIAMINS
SYQEIEDDSDVEWKFARSKLWLSYFDDGKTLPPPFSLVPSPKSFVYFIMRIVNFPKCRRR
RLQKDIEMGMGNSKSRLNLFTQSNSRVFESHSFNSILNQPTRYQQIMKRLIKRYVLKAQV
DKENDEVNEGELKEIKQDISSLRYELLEDKSQATEELAILIHKLSEKLNPSMLRCE

Ligands and cofactors

ID	Name	Formula	Copies
98R	[(2S)-2-[(E)-octadec-10-enoyl]oxy-3-oxidanyl-propyl] octadec-10-enoate	C39 H72 O5	4
POV	(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl…	C42 H82 N O8 P	4
ZN	Zinc ion	Zn	4
Y01	Cholesterol hemisuccinate	C31 H50 O4	8

Primary citation

Structural mechanism of human TRPC3 and TRPC6 channel regulation by their intracellular calcium-binding sites. Guo, W., Tang, Q., Wei, M. et al. Neuron (2022) 110:1023-1035.e5. DOI 10.1016/j.neuron.2021.12.023 · PubMed

Other PDB entries of the same protein (UniProt Q13507 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9U5C 2.25 Å, Structure of hTRPC3 in complex with Nb1-94 at 2.25 angstrom
9OLM 2.5 Å, Structure of human TRPC3 cerebellar splice variant (isoform c)
9KDB 2.67 Å, Structure of hTRPC3 in complex with Nb1-25 at 2.67 angstrom
7DXB 2.7 Å, Structure of TRPC3 at 2.7 angstrom in high calcium state
9KDD 2.7 Å, Structure of GSK1702934A-bound TRPC3 at 3.3 angstrom
9VFI 2.72 Å, Structure of hTRPC3 solubilized with 4F peptide at 2.72 angstrom
9OLK 2.8 Å, Structure of wild-type human TRPC3
9KDC 3.01 Å, Structure of hTRPC3 in complex with Nb3-37 at 3.01 angstrom
7DXC 3.06 Å, Structure of TRPC3 at 3.06 angstrom in low calcium state
9OLL 3.1 Å, Structure of human TRPC3 T573A mutant
6CUD 3.3 Å, Structure of the human TRPC3 in a lipid-occupied, closed state
9OLX 3.3 Å, Structure of a constitutively open human TRPC3 mutant in the inhibited state

Browse structure collections

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