21TQ: Sodium channel regulatory subunit beta-1

The structure of Nav1.7 with veratridine standing near the IFM motif (site I). Determined by electron microscopy at 2.7 Å resolution. Released 11 Mar 2026.

Method: Electron microscopy
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 3
Atoms: 13,098
Mol. weight: 271.91 kDa
Ligands: NAG, LPE, A1E26, Y01
Released: 11 Mar 2026

Explore 21TQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

21TQ contains 90 α-helices and 47 β-strands across 3 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: 83 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	17-33	17
α-helix	48-50	3
α-helix	51-53	3
β-strand	58	1	8
α-helix	59-60	2
α-helix	66-67	2
α-helix	68-70	3
β-strand	75	1	9
α-helix	80-84	5
β-strand	87-91	5	9
β-strand	96	1	8
β-strand	97-101	5	9
α-helix	104	1
β-strand	105	1	10
β-strand	109	1	10
α-helix	114-123	10
α-helix	126-142	17
α-helix	152-174	23
α-helix	183-185	3
α-helix	187-204	18
α-helix	210-214	5
α-helix	215-218	4
α-helix	219-227	9
α-helix	231-242	12
α-helix	246-266	21
α-helix	270-272	3
β-strand	273-277	5	11
α-helix	286-289	4
α-helix	296-299	4
β-strand	303	1	11
β-strand	305	1	12
β-strand	312	1	12
α-helix	313-314	2
β-strand	328-332	5	11
α-helix	335-336	2
α-helix	347-358	12
α-helix	363-374	12
α-helix	376-378	3
α-helix	379-384	6
α-helix	385-392	8
α-helix	393-418	26
α-helix	731-741	11
α-helix	744-761	18
β-strand	765	1	13
α-helix	770-797	28
α-helix	800-803	4
α-helix	807-823	17
α-helix	832-836	5
α-helix	837-847	11
α-helix	850-861	12
α-helix	867-894	28
α-helix	896-898	3
α-helix	913-925	13
α-helix	929-939	11
α-helix	941-971	31
α-helix	987-996	10
α-helix	1176-1189	14
α-helix	1192-1207	16
α-helix	1208-1211	4
α-helix	1214-1218	5
α-helix	1220-1248	29
α-helix	1250-1253	4
α-helix	1257-1274	18
α-helix	1275-1279	5
α-helix	1284-1290	7
α-helix	1291-1298	8
α-helix	1299-1303	5
α-helix	1305-1316	12
α-helix	1318-1343	26
β-strand	1349-1352	4	14
α-helix	1357	1
β-strand	1358	1	14
α-helix	1359-1360	2
β-strand	1366	1	15
α-helix	1367-1374	8
β-strand	1380-1383	4	14
β-strand	1391	1	13
α-helix	1392-1403	12
α-helix	1408-1416	9
β-strand	1423	1	15
α-helix	1431-1433	3
α-helix	1434-1440	7
α-helix	1441-1447	7
α-helix	1448-1462	15
α-helix	1466-1467	2
α-helix	1476-1485	10
α-helix	1486-1488	3
α-helix	1491-1500	10
α-helix	1503-1513	11
α-helix	1515-1534	20
α-helix	1541-1569	29
α-helix	1570-1575	6
α-helix	1577-1601	25
α-helix	1606-1613	8
α-helix	1614-1618	5
α-helix	1620-1626	7
α-helix	1628-1665	38
α-helix	1684-1693	10
α-helix	1694-1696	3
α-helix	1700-1704	5
α-helix	1705-1708	4
β-strand	1720	1	16
β-strand	1727	1	16
α-helix	1733-1765	33

Chain B: 4 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	24-27	4
β-strand	31	1	1
β-strand	36-38	3	2
β-strand	41	1	3
β-strand	50-61	12	4
β-strand	68-74	7	4
β-strand	77-80	4	4
β-strand	90-92	3	2
β-strand	103	1	3
β-strand	106-108	3	2
α-helix	113-115	3
β-strand	117-129	13	4
β-strand	132-138	7	4
β-strand	141-144	4	4
β-strand	147	1	1
α-helix	150-153	4
α-helix	154-191	38

Chain C: 3 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	31-33	3	5
β-strand	37-41	5	6
β-strand	46-48	3	7
β-strand	51-53	3	5
α-helix	57-58	2
β-strand	64-70	7	6
β-strand	77-83	7	6
β-strand	87-89	3	6
β-strand	99-101	3	7
β-strand	104	1	5
α-helix	105-107	3
β-strand	109	1	5
β-strand	112-114	3	7
α-helix	119-121	3
β-strand	123-130	8	6
β-strand	138-147	10	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Sodium channel regulatory subunit beta-1	B	protein	173	Homo sapiens	Q07699 (AlphaFold model)
Sodium channel regulatory subunit beta-2	C	protein	119	Homo sapiens	O60939 (AlphaFold model)
Sodium channel protein type 9 subunit alpha	A	protein	1988	Homo sapiens	Q15858 (AlphaFold model)

Sequence of entity 1 (B), FASTA

>21TQ_1 Sodium channel regulatory subunit beta-1 (chains B)
GCVEVDSETEAVYGMTFKILCISCKRRSETNAETFTEWTFRQKGTEEFVKILRYENEVLQ
LEEDERFEGRVVWNGSRGTKDLQDLSIFITNVTYNHSGDYECHVYRLLFFENYEHNTSVV
KKIHIEVVDKANRDMASIVSEIMMYVLIVVLTIWLVAEMIYCYKKIAAATETA

Sequence of entity 2 (C), FASTA

>21TQ_2 Sodium channel regulatory subunit beta-2 (chains C)
MEVTVPATLNVLNGSDARLPCTFNSCYTVNHKQFSLNWTYQECNNCSEEMFLQFRMKIIN
LKLERFQDRVEFSGNPSKYDVSVMLRNVQPEDEGIYNCYIMNPPDRHRGHGKIHLQVLM

Sequence of entity 3 (A), FASTA

>21TQ_3 Sodium channel protein type 9 subunit alpha (chains A)
MAMLPPPGPQSFVHFTKQSLALIEQRIAERKSKEPKEEKKDDDEEAPKPSSDLEAGKQLP
FIYGDIPPGMVSEPLEDLDPYYADKKTFIVLNKGKTIFRFNATPALYMLSPFSPLRRISI
KILVHSLFSMLIMCTILTNCIFMTMNNPPDWTKNVEYTFTGIYTFESLVKILARGFCVGE
FTFLRDPWNWLDFVVIVFAYLTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQ
SVKKLSDVMILTVFCLSVFALIGLQLFMGNLKHKCFRNSLENNETLESIMNTLESEEDFR
KYFYYLEGSKDALLCGFSTDSGQCPEGYTCVKIGRNPDYGYTSFDTFSWAFLALFRLMTQ
DYWENLYQQTLRAAGKTYMIFFVVVIFLGSFYLINLILAVVAMAYEEQNQANIEEAKQKE
LEFQQMLDRLKKEQEEAEAIAAAAAEYTSIRRSRIMGLSESSSETSKLSSKSAKERRNRR
KKKNQKKLSSGEEKGDAEKLSKSESEDSIRRKSFHLGVEGHRRAHEKRLSTPNQSPLSIR
GSLFSARRSSRTSLFSFKGRGRDIGSETEFADDEHSIFGDNESRRGSLFVPHRPQERRSS
NISQASRSPPMLPVNGKMHSAVDCNGVVSLVDGRSALMLPNGQLLPEVIIDKATSDDSGT
TNQIHKKRRCSSYLLSEDMLNDPNLRQRAMSRASILTNTVEELEESRQKCPPWWYRFAHK
FLIWNCSPYWIKFKKCIYFIVMDPFVDLAITICIVLNTLFMAMEHHPMTEEFKNVLAIGN
LVFTGIFAAEMVLKLIAMDPYEYFQVGWNIFDSLIVTLSLVELFLADVEGLSVLRSFRLL
RVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKIN
DDCTLPRWHMNDFFHSFLIVFRVLCGEWIETMWDCMEVAGQAMCLIVYMMVMVIGNLVVL
NLFLALLLSSFSSDNLTAIEEDPDANNLQIAVTRIKKGINYVKQTLREFILKAFSKKPKI
SREIRQAEDLNTKKENYISNHTLAEMSKGHNFLKEKDKISGFGSSVDKHLMEDSDGQSFI
HNPSLTVTVPIAPGESDLENMNAEELSSDSDSEYSKVRLNRSSSSECSTVDNPLPGEGEE
AEAEPMNSDEPEACFTDGCVWRFSCCQVNIESGKGKIWWNIRKTCYKIVEHSWFESFIVL
MILLSSGALAFEDIYIERKKTIKIILEYADKIFTYIFILEMLLKWIAYGYKTYFTNAWCW
LDFLIVDVSLVTLVANTLGYSDLGPIKSLRTLRALRPLRALSRFEGMRVVVNALIGAIPS
IMNVLLVCLIFWLIFSIMGVNLFAGKFYECINTTDGSRFPASQVPNRSECFALMNVSQNV
RWKNLKVNFDNVGLGYLSLLQVATFKGWTIIMYAAVDSVNVDKQPKYEYSLYMYIYFVVF
IIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRP
GNKIQGCIFDLVTNQAFDISIMVLICLNMVTMMVEKEGQSQHMTEVLYWINVVFIILFTG
ECVLKLISLRHYYFTVGWNIFDFVVVIISIVGMFLADLIETYFVSPTLFRVIRLARIGRI
LRLVKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKKEDGINDMFN
FETFGNSMICLFQITTSAGWDGLLAPILNSKPPDCDPKKVHPGSSVEGDCGNPSVGIFYF
VSYIIISFLVVVNMYIAVILENFSVATEESTEPLSEDDFEMFYEVWEKFDPDATQFIEFS
KLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDSLR
SQMEERFMSANPSKVSYEPITTTLKRKQEDVSATVIQRAYRRYRLRQNVKNISSIYIKDG
DRDDDLLNKKDMAFDNVNENSSPEKTDATSSTTSPPSYDSVTKPDKEKYEQDRTEKEDKG
KDSKESKK

Ligands and cofactors

ID	Name	Formula	Copies
NAG	2-acetamido-2-deoxy-beta-D-glucopyranose	C8 H15 N O6	6
LPE	1-O-octadecyl-sn-glycero-3-phosphocholine	C26 H57 N O6 P	8
A1E26	Veratridine	C36 H51 N O11	1
Y01	Cholesterol hemisuccinate	C31 H50 O4	4
PCW	1,2-dioleoyl-sn-glycero-3-phosphocholine	C44 H85 N O8 P	2
P3X	(5E,17R,20S)-23-amino-20-hydroxy-14,20-dioxo-15,19,21-trioxa-20lambda~5~-phosph…	C35 H68 N O8 P	1

Primary citation

Open-state structure of veratridine-activated human Nav1.7 reveals the molecular choreography of fast inactivation. Fan, X., Chen, J., Xue, L. et al. To be published.

Other PDB entries of the same protein (UniProt Q07699 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7W9K 2.2 Å, Cryo-EM structure of human Nav1.7-beta1-beta2 complex at 2.2 angstrom resolution
25II 2.5 Å, Cryo-EM structure of human Nav1.6 in complex with Iota-Conotoxin RXIA
8I5Y 2.6 Å, Structure of human Nav1.7 in complex with vixotrigine
7XVE 2.7 Å, Human Nav1.7 mutant class-I
8I5B 2.7 Å, Structure of human Nav1.7 in complex with bupivacaine
8I5G 2.7 Å, Structure of human Nav1.7 in complex with PF-05089771
8THH 2.7 Å, Cryo-EM structure of Nav1.7 with LTG
25IH 2.8 Å, Cryo-EM structure of human Nav1.6 in complex with Cn2
7XVF 2.8 Å, Nav1.7 mutant class2
8G1A 2.8 Å, Cryo-EM structure of Nav1.7 with CBD
8XMM 2.89 Å, Voltage-gated sodium channel Nav1.7 variant M9
7W9P 2.9 Å, Cryo-EM structure of human Nav1.7(E406K) in complex with auxiliary beta subunits,…

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