9VFI: HTRPC3 solubilized with 4F peptide

Structure of hTRPC3 solubilized with 4F peptide at 2.72 angstrom. Determined by electron microscopy at 2.72 Å resolution. Released 22 Apr 2026.

Method

Electron microscopy

Resolution

2.72 Å

Organism

Homo sapiens

Chains

4

Atoms

23,248

Mol. weight

696.51 kDa

Ligands

CA, ZN, A1L5I

Released

22 Apr 2026

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

Secondary structure: helices and β-sheets

9VFI contains 184 α-helices and 32 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: 46 helices, 8 β-strands

Molecules and chains

>9VFI_1 Green fluorescence protein,Maltose/maltodextrin-binding periplasmic protein,Short transient receptor potential channel 3,Maltose/maltodextrin-binding periplasmic protein,Short transient receptor potential channel 3,Maltose/maltodextrin-binding periplasmic protein,Short transient receptor potential channel 3 (chains A, B, C, D)
MSKGEELFTGVVPILVELDGDVNGHKFSVRGEGEGDATIGKLTLKFISTTGKLPVPWPTL
VTTLTYGVQCFSRYPDHMKRHDFFKSAMPEGYVQERTISFKDDGKYKTRAVVKFEGDTLV
NRIELKGTDFKEDGNILGHKLEYNFNSHNVYITADKQKNGIKANFTVRHNVEGSGHHHHH
HHHHHHHSSGLVPRGSGWSHPQFEKGSGDYKDDDDKGSGWSHPQFEKGSGDGSVQLADHY
QQNTPIGDGPVLLPDNHYLSTQTVLSKDPNEKRDHMVLLEFVTAAGITHGMDELYKGSMK
IEEGKLVIWINGDKGYNGLAEVGKKFEKDTGIKVTVEHPDKLEEKFPQVAATGDGPDIIF
WAHDRFGGYAQSGLLAEITPDKAFQDKLYPFTWDAVRYNGKLIAYPIAVEALSLIYNKDL
LPNPPKTWEEIPALDKELKAKGKSALMFNLQEPYFTWPLIAADGGYAFKYENGKYDIKDV
GVDNAGAKAGLTFLVDLIKNKHMNADTDYSIAEAAFNKGETAMTINGPWAWSNIDTSKVN
YGVTVLPTFKGQPSKPFVGVLSAGINAASPNKELAKEFLENYLLTDEGLEAVNKDKPLGA
VALKSYEEELVKDPRIAATMENAQKGEIMPNIPQMSAFWYAVRTAVINAASGRQTVDEAL
KDAQTGGLEVLFQGPEFGLNDIFEAQKIEWHEGSGSGSMREKGRRQAVRGPAFMFNDRGT
SLTAEEERFLDAAEYGNIPVVRKMLEESKTLNVNCVDYMGQNALQLAVGNEHLEVTELLL
KKENLARIGDALLLAISKGYVRIVEAILNHPGFAASKRLTLSPCEQELQDDDFYAYDEDG
TRFSPDITPIILAAHCQKYEVVHMLLMKGARIERPHDYFCKCGDCMEKQRHDSFSHSRSR
INAYKGLASPAYLSLSSEDPVLTALELSNELAKLANIEKEFKNDYRKLSMQCKDFVVGVL
DLCRDSEEVEAILNGDLESAEPLEVHRHKASLSRVKLAIKYEVKKFVAHPNCQQQLLTIW
YENLSGLREQTIAIKCLVVLVVALGLPFLAIGYWIAPCSRLGKILRSPFMKFVAHAASFI
IFLGLLVFNASDRFEGITTLPNITVTDYPKQIFRVKTTQFTWTEMLIMVWVLGMMWSECK
ELWLEGPREYILQLWNVLDFGMLSIFIAAFTARFLAFLQATKAQQYVDSYVQESDLSEVT
LPPEIQYFTYARDKWLPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTV
KDIFKFMVLFIMVFFAFMIGMFILYSYYLGAKVNAAFTTVEESFKTLFWSIFGLSEVTSV
VLKYDHKFIENIGYVLYGIYNVTMVVVLLNMLIAMINSSYQEIEDDSDVEWKFARSKLWL
SYFDDGKTLPPPFSLVPSPKSFVYFIMRIVNFPKCRRRRLQKDIEMGMGNSKSRLNLFTQ
SNSRVFESHSFNSILNQPTRYQQIMKRLIKRYVLKAQVDKENDEVNEGELKEIKQDISSL
RYELLEDKSQATEELAILIHKLSEKLNPSMLRCE

Ligands and cofactors

Primary citation

Unveiling Eukaryotic Membrane Proteins in High Resolution Using Peptide Solubilization. Zang, J., Shi, Y., Tao, W. et al. J Mol Biol (2025) 437:169467-169467. DOI 10.1016/j.jmb.2025.169467 · 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
• 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
• 9OLX 3.3 Å, Structure of a constitutively open human TRPC3 mutant in the inhibited state

Browse structure collections

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