7B05: TRPC4

TRPC4 in complex with inhibitor GFB-8749. Determined by electron microscopy at 3.8 Å resolution. Released 9 Dec 2020.

Method
Electron microscopy
Resolution
3.8 Å
Organism
Danio rerio
Chains
4
Atoms
21,056
Mol. weight
423.9 kDa
Ligands
SJQ, CA, 44E
Released
9 Dec 2020

Explore 7B05 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7B05 contains 160 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: 40 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix33-4210
α-helix46-5813
α-helix73-797
α-helix83-919
α-helix99-1068
α-helix109-1168
α-helix145-1517
α-helix155-16410
α-helix171-1733
α-helix189-20315
α-helix206-2116
α-helix216-23318
α-helix238-25720
α-helix262-2709
α-helix287-2948
α-helix304-31512
α-helix326-33712
α-helix340-34910
α-helix356-3605
α-helix362-38221
α-helix397-3993
α-helix401-42424
α-helix433-45826
α-helix473-49018
α-helix493-4986
α-helix503-5119
α-helix514-53825
α-helix539-5413
β-strand55111
β-strand55811
α-helix564-57310
α-helix574-5763
α-helix581-5833
α-helix593-60614
α-helix607-6115
α-helix613-62816
α-helix632-64413
α-helix699-71618
α-helix717-7226
α-helix725-7273
α-helix728-7303
α-helix732-75322

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transient receptor potential cation channel subfamily c member 4aA, B, C, Dprotein915Danio rerioU3N7D8 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>7B05_1 Transient receptor potential cation channel subfamily c member 4a (chains A, B, C, D)
GSQLYFRRTDNSSYRDRIPLRIVRAESELSTQEKSYLSAVEKGDYASVKLALEEAEIYFK
ININCIDPLGRTALLIAIENENLEIIELLLSFNVYVGDALLHAIRKEVVGAVELLLNHKK
PSGEKQVPPILLDKQFSDFTPDITPIILAAHTNNYEIIKMLVQKGVSVPQPHEVRCNCVE
CVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDPFLTAFQLSWELQELSKVENEFKAE
YEELSHQCKHFAKDLLDQTRSSRELELILNFRDDMNLLQDEANNELARLKLAIKYRQKEF
VAQPNCQQLLASRWYDEFPGWRRRHWAGKLITCVFIGLMFPLLSLCYLVAPKSRYGLFIR
KPFIKFICHTASYLTFLFLLLLASQHIVSNNPDRQGPKPTTVEWMILPWVLGFIWTEIKQ
MWDGGFQDYIHDWWNLMDFVMNSLYLATISLKIVAYVKYSGCKPRDTWEMWHPTLVAEAV
FAIANIFSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFY
YENSEGMTCKGIRCERQNNAFSTLFETLQSLFWSIFGLISLYVTNVKADHKFTEFVGATM
FGTYNVISLVVLLNMLIAMMNNSYQHIADHADIEWKFARTKLWMSYFEEGGTLPPPFNII
PSPKSICYLITWIKVHVFKRRSKRTETFGTLGRRAAENVRLNHQYQEVLRNLVKRYVAAM
IRDAKTEEGLTEENFKELKQDISSFRYEVIGMMKGNRKSTRANKSDTSASDVSHPEGSLQ
YSSALKQNSKLHLYDVTTALQQQNSEEAKASLGCLANGSAVVLTEPILKDKARSDFPKDF
TDFGLFPKKQNPNKIYSLAEEATESDPDILDWGKEDKPLAGKVEQDVNESKCLMEEDERV
LEEQEMEHIASSHEH

Ligands and cofactors

IDNameFormulaCopies
SJQ4-[4-[[4,4-bis(fluoranyl)cyclohexyl]methyl]-3-oxidanylidene-piperazin-1-yl]-5-c…C15 H19 Cl F2 N4 O24
CACalcium ionCa4
44E(2R)-3-(phosphonooxy)propane-1,2-diyl dihexanoateC15 H29 O8 P4

Primary citation

Structural basis of TRPC4 regulation by calmodulin and pharmacological agents. Vinayagam, D., Quentin, D., Yu-Strzelczyk, J. et al. Elife (2020) 9. DOI 10.7554/eLife.60603 · PubMed

Other PDB entries of the same protein (UniProt U3N7D8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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