6DJS: Hybrid model of TRPC3 in GDN

Hybrid model of TRPC3 in GDN. Determined by electron microscopy at 5.8 Å resolution. Released 29 Aug 2018.

Method: Electron microscopy
Resolution: 5.8 Å
Organism: Homo sapiens
Chains: 4
Atoms: 12,888
Mol. weight: 275.14 kDa
Released: 29 Aug 2018

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

Secondary structure: helices and β-sheets

6DJS contains 104 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.

Chains A, B, C and D: 26 helices, 0 β-strands

Element	Residues	Length
α-helix	38-48	11
α-helix	52-58	7
α-helix	77-82	6
α-helix	87-95	9
α-helix	103-111	9
α-helix	115-121	7
α-helix	163-169	7
α-helix	173-181	9
α-helix	199-202	4
α-helix	209-219	11
α-helix	226-229	4
α-helix	234-250	17
α-helix	255-273	19
α-helix	279-285	7
α-helix	290-294	5
α-helix	306-308	3
α-helix	371-390	20
α-helix	398-415	18
α-helix	425-451	27
α-helix	476-496	21
α-helix	508-532	25
α-helix	542-549	8
α-helix	564-595	32
α-helix	601-620	20
α-helix	774-794	21
α-helix	801-817	17

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Short transient receptor potential channel 3	A, B, C, D	protein	676	Homo sapiens	Q13507 (AlphaFold model)

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

>6DJS_1 Short transient receptor potential channel 3 (chains A, B, C, D)
GAMGSMEGSPSLRRMTVMREKGRRQAVRGPAFMFNDRGTSLTAEEERFLDAAEYGNIPVV
RKMLEESKTLNVNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARIGDALLLAISKGYV
RIVEAILNHPGFAASKRLTLSPCEQELQDDDFYAYDEDGTRFSPDITPIILAAHCQKYEV
VHMLLMKGARIERPHDYFCKCGDCMEKQRHDSFSHSRSRINAYKGLASPAYLSLSSEDPV
LTALELSNELAKLANIEKEFKNDYRKLSMQCKDFVVGVLDLCRDSEEVEAILNGDLESAE
PLEVHRHKASLSRVKLXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
XXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXXX
TRYQQIMKRLIKRYVLKAQVDKENDEVNEGELKEIKQDISSLRYELLEDKSQATEELAIL
IHKLSEKLNPSMLRCE

Primary citation

Structure-function analyses of the ion channel TRPC3 reveal that its cytoplasmic domain allosterically modulates channel gating. Sierra-Valdez, F., Azumaya, C.M., Romero, L.O. et al. J Biol Chem (2018) 293:16102-16114. DOI 10.1074/jbc.RA118.005066 · 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

Browse structure collections

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