9KDC: HTRPC3

Structure of hTRPC3 in complex with Nb3-37 at 3.01 angstrom. Determined by electron microscopy at 3.01 Å resolution. Released 8 Oct 2025.

Method

Electron microscopy

Resolution

3.01 Å

Organisms

Homo sapiens, Camelus

Chains

6

Atoms

25,065

Mol. weight

462.04 kDa

Ligands

ZN, CA, A1L5I

Released

8 Oct 2025

Explore 9KDC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9KDC contains 165 α-helices and 48 β-strands across 6 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: 40 helices, 6 β-strands

Molecules and chains

>9KDC_1 Short transient receptor potential channel 3 (chains A, B, C, D)
MSTKVRKCKEQARVTFPAPEEEEDEGEDEGAEPQRRRRGWRGVNGGLEPRSAPSQREPHG
YCPPPFSHGPDLSMEGSPSLRRMTVMREKGRRQAVRGPAFMFNDRGTSLTAEEERFLDAA
EYGNIPVVRKMLEESKTLNVNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARIGDALL
LAISKGYVRIVEAILNHPGFAASKRLTLSPCEQELQDDDFYAYDEDGTRFSPDITPIILA
AHCQKYEVVHMLLMKGARIERPHDYFCKCGDCMEKQRHDSFSHSRSRINAYKGLASPAYL
SLSSEDPVLTALELSNELAKLANIEKEFKNDYRKLSMQCKDFVVGVLDLCRDSEEVEAIL
NGDLESAEPLEVHRHKASLSRVKLAIKYEVKKFVAHPNCQQQLLTIWYENLSGLREQTIA
IKCLVVLVVALGLPFLAIGYWIAPCSRLGKILRSPFMKFVAHAASFIIFLGLLVFNASDR
FEGITTLPNITVTDYPKQIFRVKTTQFTWTEMLIMVWVLGMMWSECKELWLEGPREYILQ
LWNVLDFGMLSIFIAAFTARFLAFLQATKAQQYVDSYVQESDLSEVTLPPEIQYFTYARD
KWLPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVLFIMV
FFAFMIGMFILYSYYLGAKVNAAFTTVEESFKTLFWSIFGLSEVTSVVLKYDHKFIENIG
YVLYGIYNVTMVVVLLNMLIAMINSSYQEIEDDSDVEWKFARSKLWLSYFDDGKTLPPPF
SLVPSPKSFVYFIMRIVNFPKCRRRRLQKDIEMGMGNSKSRLNLFTQSNSRVFESHSFNS
ILNQPTRYQQIMKRLIKRYVLKAQVDKENDEVNEGELKEIKQDISSLRYELLEDKSQATE
ELAILIHKLSEKLNPSMLRCE

>9KDC_2 Nb3-37 (chains E, F)
GPEFQVQLQESGGGSVQSGGSLRLSCAASGYTYSRSCLGWFRQAPGKERERVATIDSDGS
TSYADSVKGRFTISQDNAKNTLYLQMNSLKSEDTAMYYCASKYGSRCQNSLGYMYRGQGT
QVTVSSLEIEEQKLISEEDLGSGPSRLEEELRRRLTEHHHHHH

Ligands and cofactors

Primary citation

Structural mechanism of the agonist binding on human TRPC3 channel. Chen, Y., Zang, J., Guo, W. et al. Nat Commun (2025) 16:9343-9343. DOI 10.1038/s41467-025-64435-6 · PubMed

Related structures

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
• 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
• 9OLX 3.3 Å, Structure of a constitutively open human TRPC3 mutant in the inhibited state

Browse structure collections

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