6CUD: Human TRPC3 in a lipid-occupied, closed state

Structure of the human TRPC3 in a lipid-occupied, closed state. Determined by electron microscopy at 3.3 Å resolution. Released 16 May 2018.

Method: Electron microscopy
Resolution: 3.3 Å
Organism: Homo sapiens
Chains: 4
Atoms: 21,028
Mol. weight: 374.45 kDa
Ligands: 6OE, FGJ, NAG
Released: 16 May 2018

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

Secondary structure: helices and β-sheets

6CUD contains 172 α-helices and 8 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 and C: 43 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	26-37	12
α-helix	40-49	10
α-helix	65-71	7
α-helix	75-81	7
α-helix	92-99	8
α-helix	104-110	7
α-helix	113-116	4
α-helix	151-158	8
α-helix	161-170	10
α-helix	174-177	4
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	268-274	7
α-helix	295-302	8
α-helix	306-309	4
α-helix	312-322	11
α-helix	329-331	3
α-helix	334-346	13
α-helix	348-350	3
α-helix	351-356	6
α-helix	358-360	3
α-helix	362-365	4
α-helix	370-391	22
α-helix	415-420	6
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	522-536	15
α-helix	539-543	5
α-helix	552-586	35
α-helix	587-589	3
β-strand	594	1	1
α-helix	602-611	10
α-helix	612-614	3
α-helix	619-621	3
β-strand	624	1	1
α-helix	629-664	36
α-helix	669-684	16
α-helix	762-784	23
α-helix	788-805	18

Chains B and D: 43 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	26-37	12
α-helix	40-49	10
α-helix	65-71	7
α-helix	75-81	7
α-helix	92-99	8
α-helix	104-110	7
α-helix	113-116	4
α-helix	151-158	8
α-helix	161-170	10
α-helix	174-177	4
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	268-274	7
α-helix	295-302	8
α-helix	306-309	4
α-helix	312-322	11
α-helix	329-331	3
α-helix	334-346	13
α-helix	348-350	3
α-helix	351-356	6
α-helix	358-360	3
α-helix	362-365	4
α-helix	370-391	22
α-helix	415-420	6
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	522-536	15
α-helix	539-543	5
α-helix	552-586	35
α-helix	587-589	3
β-strand	594	1	2
α-helix	602-611	10
α-helix	612-614	3
α-helix	619-621	3
β-strand	624	1	2
α-helix	629-664	36
α-helix	669-684	16
α-helix	762-785	24
α-helix	788-805	18

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Short transient receptor potential channel 3	A, B, C, D	protein	806	Homo sapiens	Q13507 (AlphaFold model)

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

>6CUD_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
DKENDEVNEGELKEIKQDISSLRYEL

Ligands and cofactors

ID	Name	Formula	Copies
6OE	(2S)-3-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-2-(hexanoyloxy)propyl…	C17 H34 N O8 P	4
FGJ	(2R)-3-hydroxypropane-1,2-diyl dihexanoate	C15 H28 O5	4
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	4

Primary citation

Structure of the human lipid-gated cation channel TRPC3. Fan, C., Choi, W., Sun, W. et al. Elife (2018) 7. DOI 10.7554/eLife.36852 · 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
7DXE 3.2 Å, Structure of TRPC3 gain of function mutation R803C at 3.2 angstrom in 1340nM free…
9OLX 3.3 Å, Structure of a constitutively open human TRPC3 mutant in the inhibited state

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