5ZBG: Human TRPC3

Cryo-EM structure of human TRPC3 at 4.36A resolution. Determined by electron microscopy at 4.36 Å resolution. Released 9 May 2018.

Method: Electron microscopy
Resolution: 4.36 Å
Organism: Homo sapiens
Chains: 4
Atoms: 21,260
Mol. weight: 389.86 kDa
Released: 9 May 2018

Explore 5ZBG in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5ZBG contains 152 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, B, C and D: 38 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	27-36	10
α-helix	40-49	10
α-helix	65-71	7
α-helix	75-82	8
α-helix	90-100	11
α-helix	103-110	8
α-helix	138-140	3
α-helix	151-157	7
α-helix	161-169	9
α-helix	173-179	7
α-helix	185-189	5
α-helix	198-209	12
α-helix	212-217	6
α-helix	222-239	18
α-helix	244-263	20
α-helix	268-275	8
α-helix	296-303	8
α-helix	306-309	4
α-helix	312-322	11
α-helix	335-345	11
α-helix	348-357	10
α-helix	362-366	5
α-helix	370-392	23
α-helix	424-446	23
α-helix	449-454	6
α-helix	457-488	32
α-helix	522-539	18
α-helix	540-544	5
α-helix	552-586	35
β-strand	594	1	1
α-helix	602-611	10
α-helix	619-621	3
β-strand	624	1	1
α-helix	629-642	14
α-helix	643-649	7
α-helix	650-663	14
α-helix	669-682	14
α-helix	762-781	20
α-helix	782-784	3
α-helix	789-827	39

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Short transient receptor potential channel 3	A, B, C, D	protein	848	Homo sapiens	Q13507 (AlphaFold model)

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

>5ZBG_1 Short transient receptor potential channel 3 (chains A, B, C, D)
MEGSPSLRRMTVMREKGRRQAVRGPAFMFNDRGTSLTAEEERFLDAAEYGNIPVVRKMLE
ESKTLNVNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARIGDALLLAISKGYVRIVEA
ILNHPGFAASKRLTLSPCEQELQDDDFYAYDEDGTRFSPDITPIILAAHCQKYEVVHMLL
MKGARIERPHDYFCKCGDCMEKQRHDSFSHSRSRINAYKGLASPAYLSLSSEDPVLTALE
LSNELAKLANIEKEFKNDYRKLSMQCKDFVVGVLDLCRDSEEVEAILNGDLESAEPLEVH
RHKASLSRVKLAIKYEVKKFVAHPNCQQQLLTIWYENLSGLREQTIAIKCLVVLVVALGL
PFLAIGYWIAPCSRLGKILRSPFMKFVAHAASFIIFLGLLVFNASDRFEGITTLPNITVT
DYPKQIFRVKTTQFTWTEMLIMVWVLGMMWSECKELWLEGPREYILQLWNVLDFGMLSIF
IAAFTARFLAFLQATKAQQYVDSYVQESDLSEVTLPPEIQYFTYARDKWLPSDPQIISEG
LYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVLFIMVFFAFMIGMFILYS
YYLGAKVNAAFTTVEESFKTLFWSIFGLSEVTSVVLKYDHKFIENIGYVLYGIYNVTMVV
VLLNMLIAMINSSYQEIEDDSDVEWKFARSKLWLSYFDDGKTLPPPFSLVPSPKSFVYFI
MRIVNFPKCRRRRLQKDIEMGMGNSKSRLNLFTQSNSRVFESHSFNSILNQPTRYQQIMK
RLIKRYVLKAQVDKENDEVNEGELKEIKQDISSLRYELLEDKSQATEELAILIHKLSEKL
NPSMLRCE

Primary citation

Structure of the receptor-activated human TRPC6 and TRPC3 ion channels. Tang, Q., Guo, W., Zheng, L. et al. Cell Res (2018) 28:746-755. DOI 10.1038/s41422-018-0038-2 · 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…
6CUD 3.3 Å, Structure of the human TRPC3 in a lipid-occupied, closed state

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