6JZO: Mouse TRPC4 ion channel

Structure of the mouse TRPC4 ion channel. Determined by electron microscopy at 3.28 Å resolution. Released 21 Oct 2020.

Method: Electron microscopy
Resolution: 3.28 Å
Organism: Mus musculus
Chains: 4
Atoms: 21,405
Mol. weight: 354.88 kDa
Ligands: Y01, LPP
Released: 21 Oct 2020

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

Secondary structure: helices and β-sheets

6JZO contains 137 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.

Chain A: 34 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	17-19	3	1
α-helix	31-39	9
α-helix	45-55	11
α-helix	74-79	6
α-helix	83-91	9
α-helix	99-105	7
α-helix	111-115	5
α-helix	145-152	8
α-helix	155-162	8
β-strand	168-169	2	2
α-helix	190-203	14
α-helix	216-233	18
α-helix	238-256	19
α-helix	263-268	6
α-helix	287-294	8
α-helix	306-314	9
α-helix	321-323	3
α-helix	326-338	13
α-helix	340-345	6
α-helix	354-358	5
α-helix	362-383	22
α-helix	401-421	21
α-helix	425-431	7
α-helix	433-456	24
α-helix	473-489	17
α-helix	492-498	7
α-helix	503-541	39
α-helix	564-573	10
α-helix	581-584	4
α-helix	591-605	15
α-helix	606-612	7
α-helix	613-627	15
α-helix	632-643	12
α-helix	655-657	3
α-helix	693-726	34
α-helix	733-754	22

Chain B: 35 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	17-18	2	3
α-helix	27-30	4
α-helix	31-39	9
α-helix	47-53	7
α-helix	76-79	4
α-helix	83-91	9
α-helix	99-105	7
α-helix	111-115	5
α-helix	145-152	8
α-helix	155-162	8
β-strand	167-169	3	1
α-helix	190-203	14
α-helix	216-233	18
α-helix	238-256	19
α-helix	263-268	6
α-helix	287-294	8
α-helix	306-314	9
α-helix	321-323	3
α-helix	326-338	13
α-helix	340-345	6
α-helix	354-358	5
α-helix	362-383	22
α-helix	401-421	21
α-helix	425-431	7
α-helix	433-456	24
α-helix	473-489	17
α-helix	492-498	7
α-helix	503-541	39
α-helix	564-573	10
α-helix	581-584	4
α-helix	591-605	15
α-helix	606-612	7
α-helix	613-628	16
α-helix	631-643	13
α-helix	655-657	3
α-helix	693-726	34
α-helix	733-754	22

Chain C: 34 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	17-18	2	4
α-helix	31-39	9
α-helix	47-55	9
α-helix	73-79	7
α-helix	83-91	9
α-helix	99-105	7
α-helix	111-115	5
α-helix	145-152	8
α-helix	155-162	8
β-strand	168-169	2	3
α-helix	190-203	14
α-helix	216-233	18
α-helix	238-256	19
α-helix	263-268	6
α-helix	287-294	8
α-helix	306-314	9
α-helix	321-323	3
α-helix	326-338	13
α-helix	340-345	6
α-helix	354-358	5
α-helix	362-383	22
α-helix	401-421	21
α-helix	425-431	7
α-helix	433-456	24
α-helix	473-489	17
α-helix	492-498	7
α-helix	503-541	39
α-helix	564-573	10
α-helix	582-584	3
α-helix	591-605	15
α-helix	606-612	7
α-helix	613-627	15
α-helix	631-643	13
α-helix	655-657	3
α-helix	693-726	34
α-helix	733-754	22

Chain D: 34 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	17-18	2	2
α-helix	31-39	9
α-helix	47-55	9
α-helix	73-79	7
α-helix	83-91	9
α-helix	99-105	7
α-helix	111-115	5
α-helix	145-152	8
α-helix	155-162	8
β-strand	168-169	2	4
α-helix	190-203	14
α-helix	216-233	18
α-helix	238-256	19
α-helix	262-268	7
α-helix	287-294	8
α-helix	306-314	9
α-helix	321-323	3
α-helix	326-338	13
α-helix	340-345	6
α-helix	354-358	5
α-helix	362-383	22
α-helix	401-421	21
α-helix	425-431	7
α-helix	433-456	24
α-helix	473-489	17
α-helix	492-498	7
α-helix	503-541	39
α-helix	564-573	10
α-helix	581-584	4
α-helix	591-605	15
α-helix	606-612	7
α-helix	613-627	15
α-helix	631-643	13
α-helix	655-657	3
α-helix	693-726	34
α-helix	733-754	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Short transient receptor potential channel 4	A, B, C, D	protein	755	Mus musculus	Q9QUQ5 (AlphaFold model)

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

>6JZO_1 Short transient receptor potential channel 4 (chains A, B, C, D)
MAQFYYKRNVNAPYRDRIPLRIVRAESELSPSEKAYLNAVEKGDYASVKKSLEEAEIYFK
ININCIDPLGRTALLIAIENENLELIELLLSFNVYVGDALLHAIRKEVVGAVELLLNHKK
PSGEKQVPPILLDKQFSEFTPDITPIILAAHTNNYEIIKLLVQKGVSVPRPHEVRCNCVE
CVSSSDVDSLRHSRSRLNIYKALASPSLIALSSEDPFLTAFQLSWELQELSKVENEFKSE
YEELSRQCKQFAKDLLDQTRSSRELEIILNYRDDNSLIEEQSGNDLARLKLAIKYRQKEF
VAQPNCQQLLASRWYDEFPGWRRRHWAVKMVTCFIIGLLFPVFSVCYLIAPKSPLGLFIR
KPFIKFICHTASYLTFLFLLLLASQHIDRSDLNRQGPPPTIVEWMILPWVLGFIWGEIKQ
MWDGGLQDYIHDWWNLMDFVMNSLYLATISLKIVAFVKYSALNPRESWDMWHPTLVAEAL
FAIANIFSSLRLISLFTANSHLGPLQISLGRMLLDILKFLFIYCLVLLAFANGLNQLYFY
YEETKGLSCKGIRCEKQNNAFSTLFETLQSLFWSIFGLINLYVTNVKAQHEFTEFVGATM
FGTYNVISLVVLLNMLIAMMNNSYQLIADHADIEWKFARTKLWMSYFEEGGTLPTPFNVI
PSPKSLWYLVKWIWTHLCKKKMRRKPESFGTIGRRAADNLRRHHQYQEVMRNLVKRYVAA
MIREAKTEEGLTEENVKELKQDISSFRFEVLGLLR

Ligands and cofactors

ID	Name	Formula	Copies
Y01	Cholesterol hemisuccinate	C31 H50 O4	4
LPP	2-(hexadecanoyloxy)-1-[(phosphonooxy)methyl]ethyl hexadecanoate	C35 H69 O8 P	4

Water and common crystallization additives (NA) are not listed.

Primary citation

Structure of the mouse TRPC4 ion channel. Duan, J., Li, J., Zeng, B. et al. To be published.

Other PDB entries of the same protein (UniProt Q9QUQ5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7CQP 1.9 Å, Complex of TRPC4 and Calmodulin_Nlobe
5Z96 3.28 Å, Structure of the mouse TRPC4 ion channel

Browse structure collections

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