CODSWALLOP

Sodium channel protein type 10 subunit alpha

Homo sapiens · seed Q9Y5Y9 · 1956 aa · family defined as ≥30% identity to that seed · compiled 07 October 2026

CATH and SCOP identifiers come from the RCSB's own structure annotations, which the Domains panel already reads, so these are looked up rather than guessed at.

101Entries 101Entities 47Constructs 7Organisms 83Ligand-bound
1.35 ÅBest res.
3.10 ÅMedian res.

Every figure here is counted over the whole family rather than quoted from one entry.

The reference structure

7WE4, the structure every other member of this family is superposed onto. Rendered by the RCSB and embedded here: the live app shows an interactive viewport, which a document that fetches nothing cannot.

Rendered structure of 7WE4
7WE4 at the RCSB · open it in the 3D viewer

Which residues anyone has ever seen

How many of this family's constructs contain each residue of the seed. A trough is a stretch nobody has put in a construct, which is a construct-design answer rather than a disorder one.

1978195691 constructs

Constructs, most-used first

47 distinct constructs across 101 entries. 81 polymer entities differ from the UniProt canonical sequence in some way, 55 carry a recognised expression tag and 10 carry a fusion partner.

"Differs from canonical" is not the same as "engineered". The canonical sequence is the full gene product, so a secreted protein whose structures all start after its signal peptide counts every one of them as different: lysozyme's most-used construct, residues 19–147 on 1,239 entities, is simply the mature protein. Read the construct column below for what was actually done, rather than this count.

EntitiesLengthBest (Å)Best entryWhat was made
8 1988 2.70 21TQ matches the canonical sequence
8 2031 2.90 7W9P FLAG+Strep-II; E406K
7 1596 2.60 6A95 FLAG+Strep-II
7 1980 2.50 25II matches the canonical sequence
4 1608 2.20 8F0P FLAG+Strep-II; F270S, V274L, L275I +78 more
4 1838 3.24 6UZ0 fused to GFP (internal); residues 1-1906; 2 internal deletions; 13-residue insertion after 1899; R1899E, R1900Y, H1902D +4 more
4 1956 2.70 7WE4 S894F
4 2001 2.76 9DBN FLAG+Strep-II; TEV site; M1713V
4 2028 2.60 8I5Y FLAG+Strep-II
3 288 3.54 6N4I FLAG; Thrombin site; 1 internal deletion; 4-residue insertion after 89; G26T, I27L, T28F +39 more
3 296 2.60 8VGL FLAG; Thrombin site; 2 internal deletions; 14-residue insertion after 89; G26M, I27V, G30M +29 more
3 2016 3.48 9P24 matches the canonical sequence
3 2250 3.07 7XMF Strep-II; fused to GFP; 3C/PreScission site; 1 internal deletion; W1161R
2 277 3.20 6W6O residues 722-1010; 2 internal deletions; 1-residue insertion after 767; L722M, I723K, W724M +186 more
2 1559 3.40 6NT3 FLAG+Strep-II; residues 1-1505; F270S, V274L, L275I +78 more
2 1737 2.90 7TJ9 FLAG+Strep-II
2 2022 2.70 7XVE FLAG+Strep-II; E156K, G779R, L866F +8 more
2 2059 3.30 6LQA FLAG+Strep-II
1 35 1.35 4DJC residues 1488-1522; T1488S, E1489N, E1490A
1 51 2.25 5DBR residues 1479-1529; K1479G, L1480P, G1482S
1 53 residues 1474-1526
1 97 residues 1769-1865; A1769G, I1770P, I1771G +1 more
1 129 residues 1751-1882; 2 internal deletions; V1751M, I1753S, F1754S +15 more
1 140 2.69 6MUD residues 1783-1922; T1783S, E1784N, P1785A
1 157 2.80 4OVN residues 1773-1929

Showing the 25 most-used of 47.

Positions people deliberately mutate

Columns where the wild-type residue still dominates but a real minority carries something else, which is a different question from "what varies across species".

R52K 70% P548Q 70% P550S 70% L1682V 70% D1093L 70% S1870N 70% S1772D 70% K26Q 70% I462R 70% D480S 70% P937S 70% E1892K 70% H961Y 70% S348A 69% D903E 69% F135L 69% D1331E 69% F1468C 69% W1634K 69% G469S 69% R923Y 69% N1686S 68% T1081S 68% L1185I 68% P980S 68% P901I 68% V1137I 68% R1847K 68% E420Q 68% M424R 68%

What it assembles into

Oligomeric stateChainsEntriesShare
trimeric3 39 38.6%
monomeric1 28 27.7%
dimeric2 24 23.8%
octameric8 5 5.0%
tetrameric4 2 2.0%
dodecameric12 2 2.0%
pentameric5 1 1.0%

18 entries have the depositor's assembly corroborated by PISA, 83 carry the depositor's word alone and 0 were assigned by PISA where the depositor gave none. The middle figure is not a disagreement: PISA may have returned nothing or never run. 1 entries carry more than one assembly with different chain counts, so they have no single answer to quote: 4DCK.

Domain architecture

Every source's own domains on the seed axis, one row each. They are not merged: Pfam, CATH, SCOP and InterPro disagree about boundaries, and a merged track would state a consensus none of them gave.

CATHImmunoglobulinsVoltage-gated potassium chEF-hand19781956
DomainSourceSpan (seed)Chains
ImmunoglobulinsCATH 2.60.40.10 40–159 5
Voltage-gated potassium channels. Chain CCATH 1.20.120.350 883–1022 9
1.10.287.70CATH 1293–1382 5
EF-handCATH 1.10.238.10 1727–1844 8
iswi atpaseCATH 1.20.5.1190 1846–1878 3

What binds it

NAG NAG75 entries LPE LPE36 entries P5S P5S29 entries 9Z9 9Z926 entries 6OU 6OU13 entries 1PW 1PW7 entries P3X P3X5 entries 9SL 9SL5 entries 9SR 9SR5 entries POV POV4 entries 95T 95T3 entries BMA BMA3 entries
ComponentClassNameEntriesBest (Å)
NAGcofactor 2-Acetamido-2-Deoxy-Beta-D-Glucopyranose 75 2.20
LPEligand 1-O-Octadecyl-Sn-Glycero-3-Phosphocholine 36 2.20
Y01lipid/detergent Cholesterol Hemisuccinate 35 2.20
PCWlipid/detergent 1,2-Dioleoyl-Sn-Glycero-3-Phosphocholine 35 2.20
P5Sligand O-[(R)-{[(2r)-2,3-Bis(Octadecanoyloxy)propyl]oxy}(Hydroxy)phosph 29 2.20
9Z9ligand (3beta,14beta,17beta,25r)-3-[4-Methoxy-3-(Methoxymethyl)butoxy]s 26 2.20
CLRlipid/detergent Cholesterol 17 2.50
6OUligand [(2~{R})-1-[2-Azanylethoxy(Oxidanyl)phosphoryl]oxy-3-Hexadecanoy 13 3.20
NAion Sodium Ion 11 2.20
1PWligand (2s,3r,4e)-2-(Acetylamino)-3-Hydroxyoctadec-4-En-1-Yl Dihydrogen 7 2.20
CAion Calcium Ion 6 1.35
P3Xligand (5e,17r,20s)-23-Amino-20-Hydroxy-14,20-Dioxo-15,19,21-Trioxa-20l 5 2.50
9SLligand [(3as,4r,10as)-2,6-Diamino-10,10-Dihydroxy-3a,4,9,10-Tetrahydro- 5 2.90
9SRligand (1r,5r,6r,7r,9s,11s,12s,13s,14s)-3-Amino-14-(Hydroxymethyl)-8,10 5 2.60
POVligand (2s)-3-(Hexadecanoyloxy)-2-[(9z)-Octadec-9-Enoyloxy]propyl 2-(Tr 4 2.90
PEElipid/detergent 1,2-Dioleoyl-Sn-Glycero-3-Phosphoethanolamine 4 2.20
95Tligand 5-(4-Chlorophenyl)-~{N}-(3,5-Dimethoxyphenyl)furan-2-Carboxamide 3 2.70
BMAcofactor Beta-D-Mannopyranose 3 2.50
A1E26ligand Veratridine 2 2.70
MGion Magnesium Ion 2 2.20

How it crystallises

Parsed from the free text 11 depositors typed into _exptl_crystal_grow.pdbx_details, out of 11 entries that recorded anything at all. Median pH 6.5 (range 4.0 to 9.5).

Precipitants

PEG × Isopropanol × Calcium chloride × Ammonium sulfate × Sodium malonate × Sodium citrate × Magnesium chloride ×

Buffers

MES × Tris × Sodium cacodylate × Sodium acetate × Citrate × HEPES ×

Which entries to trust

101 entries carry a wwPDB validation report: 65 clean, 20 worth a check and 16 with something to explain. Median clashscore 10.6, median RSRZ outliers 1.89%, median R-free minus R-work 0.034. 100 have released structure factors.

Across species

OrganismEntriesBest (Å)Ligand-boundSeed covered
Homo sapiens75 1.35 64 100%
Periplaneta americana9 2.60 9 93%
Rattus norvegicus8 3.20 7 95%
Aliarcobacter butzleri RM40185 2.60 1 22%
Halalkalibacterium halodurans C-1252 3.20 2 14%
Escherichia coli K-121 3.60 0 8%
Electrophorus electricus1 4.00 0 95%

Seed sequence

1956 residues, numbered every ten. Every identity figure in this document is measured against this sequence.

active or binding site modified residue or glycosylation disulphide cysteine transmembrane or signal the 15 most-substituted positions

1MEFPIGSLET NNFRRFTPES LVEIEKQIAA KQGTKKAREK HREQKDQEEK PRPQLDLKAC
61NQLPKFYGEL PAELIGEPLE DLDPFYSTHR TFMVLNKGRT ISRFSATRAL WLFSPFNLIR
121RTAIKVSVHS WFSLFITVTI LVNCVCMTRT DLPEKIEYVF TVIYTFEALI KILARGFCLN
181EFTYLRDPWN WLDFSVITLA YVGTAIDLRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI
241HSVKKLADVT ILTIFCLSVF ALVGLQLFKG NLKNKCVKND MAVNETTNYS SHRKPDIYIN
301KRGTSDPLLC GNGSDSGHCP DGYICLKTSD NPDFNYTSFD SFAWAFLSLF RLMTQDSWER
361LYQQTLRTSG KIYMIFFVLV IFLGSFYLVN LILAVVTMAY EEQNQATTDE IEAKEKKFQE
421ALEMLRKEQE VLAALGIDTT SLHSHNGSPL TSKNASERRH RIKPRVSEGS TEDNKSPRSD
481PYNQRRMSFL GLASGKRRAS HGSVFHFRSP GRDISLPEGV TDDGVFPGDH ESHRGSLLLG
541GGAGQQGPLP RSPLPQPSNP DSRHGEDEHQ PPPTSELAPG AVDVSAFDAG QKKTFLSAEY
601LDEPFRAQRA MSVVSIITSV LEELEESEQK CPPCLTSLSQ KYLIWDCCPM WVKLKTILFG
661LVTDPFAELT ITLCIVVNTI FMAMEHHGMS PTFEAMLQIG NIVFTIFFTA EMVFKIIAFD
721PYYYFQKKWN IFDCIIVTVS LLELGVAKKG SLSVLRSFRL LRVFKLAKSW PTLNTLIKII
781GNSVGALGNL TIILAIIVFV FALVGKQLLG ENYRNNRKNI SAPHEDWPRW HMHDFFHSFL
841IVFRILCGEW IENMWACMEV GQKSICLILF LTVMVLGNLV VLNLFIALLL NSFSADNLTA
901PEDDGEVNNL QVALARIQVF GHRTKQALCS FFSRSCPFPQ PKAEPELVVK LPLSSSKAEN
961HIAANTARGS SGGLQAPRGP RDEHSDFIAN PTVWVSVPIA EGESDLDDLE DDGGEDAQSF
1021QQEVIPKGQQ EQLQQVERCG DHLTPRSPGT GTSSEDLAPS LGETWKDESV PQVPAEGVDD
1081TSSSEGSTVD CLDPEEILRK IPELADDLEE PDDCFTEGCI RHCPCCKLDT TKSPWDVGWQ
1141VRKTCYRIVE HSWFESFIIF MILLSSGSLA FEDYYLDQKP TVKALLEYTD RVFTFIFVFE
1201MLLKWVAYGF KKYFTNAWCW LDFLIVNISL ISLTAKILEY SEVAPIKALR TLRALRPLRA
1261LSRFEGMRVV VDALVGAIPS IMNVLLVCLI FWLIFSIMGV NLFAGKFWRC INYTDGEFSL
1321VPLSIVNNKS DCKIQNSTGS FFWVNVKVNF DNVAMGYLAL LQVATFKGWM DIMYAAVDSR
1381EVNMQPKWED NVYMYLYFVI FIIFGGFFTL NLFVGVIIDN FNQQKKKLGG QDIFMTEEQK
1441KYYNAMKKLG SKKPQKPIPR PLNKFQGFVF DIVTRQAFDI TIMVLICLNM ITMMVETDDQ
1501SEEKTKILGK INQFFVAVFT GECVMKMFAL RQYYFTNGWN VFDFIVVVLS IASLIFSAIL
1561KSLQSYFSPT LFRVIRLARI GRILRLIRAA KGIRTLLFAL MMSLPALFNI GLLLFLVMFI
1621YSIFGMSSFP HVRWEAGIDD MFNFQTFANS MLCLFQITTS AGWDGLLSPI LNTGPPYCDP
1681NLPNSNGTRG DCGSPAVGII FFTTYIIISF LIMVNMYIAV ILENFNVATE ESTEPLSEDD
1741FDMFYETWEK FDPEATQFIT FSALSDFADT LSGPLRIPKP NRNILIQMDL PLVPGDKIHC
1801LDILFAFTKN VLGESGELDS LKANMEEKFM ATNLSKSSYE PIATTLRWKQ EDISATVIQK
1861AYRSYVLHRS MALSNTPCVP RAEEEAASLP DEGFVAFTAN ENCVLPDKSE TASATSFPPS
1921YESVTRGLSD RVNMRTSSSI QNEDEATSME LIAPGP

Sites are UniProt's curated features where the seed is a UniProt accession; the substituted positions are measured from this family's own alignment rather than annotated, and only the fifteen most substituted are marked: every position carrying a minority substitution would be most of the protein, because the family holds orthologues. A residue can carry more than one and is drawn with the first that applies, in the order of the key above.

Primary citations

One record per paper, not per entry.

YearCitation
2026 Diverse binding poses of agonistic neurotoxins on human Na v 1.6. Nature doi:10.1038/s41586-026-10661-x
2026 Optical control of the cardiac rhythm with photoswitchable Na V 1.5 channel blockers. Nat Commun doi:10.1038/s41467-026-70305-6
2026 Structural and functional mechanisms underlying activation gate dynamics and IFM motif accessibility in human Na v 1.5. Nat Commun doi:10.1038/s41467-026-69672-x
2025 Structural basis of inhibition of human Na V 1.8 by the tarantula venom peptide Protoxin-I. Nat Commun doi:10.1038/s41467-024-55764-z
2025 Critical role of extracellular loops in differential modulations of TTX-sensitive and TTX-resistant Na v channels. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2510355122
2025 Structural basis of human Na v 1.5 gating mechanisms. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2416181122
2024 Disulfi de constrained Fabs overcome target size limitation for high-resolution single-particle cryo-EM. Biorxiv doi:10.1101/2024.05.10.593593
2024 Dissection of the structure-function relationship of Na v channels. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2322899121
2024 Dual receptor-sites reveal the structural basis for hyperactivation of sodium channels by poison-dart toxin batrachotoxin. Nat Commun doi:10.1038/s41467-024-45958-w
2024 Scorpion alpha-toxin Lqh alpha IT specifically interacts with a glycan at the pore domain of voltage-gated sodium channels. Structure doi:10.1016/j.str.2024.07.021
2023 Cryo-EM reveals an unprecedented binding site for Na V 1.7 inhibitors enabling rational design of potent hybrid inhibitors. Elife doi:10.7554/eLife.84151
2023 Structural mapping of Na v 1.7 antagonists. Nat Commun doi:10.1038/s41467-023-38942-3
2023 Dual-pocket inhibition of Na v channels by the antiepileptic drug lamotrigine. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2309773120
2023 Cannabidiol inhibits Na v channels through two distinct binding sites. Nat Commun doi:10.1038/s41467-023-39307-6
2023 Cryo-EM structure of human voltage-gated sodium channel Na v 1.6. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2220578120
2023 Structural basis for inhibition of the cardiac sodium channel by the atypical antiarrhythmic drug ranolazine. Nat Cardiovasc Res doi:10.1038/s44161-023-00271-5
2023 Structure of human Na V 1.6 channel reveals Na + selectivity and pore blockade by 4,9-anhydro-tetrodotoxin. Nat Commun doi:10.1038/s41467-023-36766-9
2022 High-resolution structures of human Na v 1.7 reveal gating modulation through alpha-pi helical transition of S6 IV. Cell Rep doi:10.1016/j.celrep.2022.110735
2022 Structural basis for high-voltage activation and subtype-specific inhibition of human Na v 1.8. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2208211119
2022 Unwinding and spiral sliding of S4 and domain rotation of VSD during the electromechanical coupling in Na v 1.7. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2209164119
2022 Structure-guided unlocking of Na X reveals a non-selective tetrodotoxin-sensitive cation channel. Nat Commun doi:10.1038/s41467-022-28984-4
2022 Structural basis for Na V 1.7 inhibition by pore blockers. Nat.Struct.Mol.Biol. doi:10.1038/s41594-022-00860-1
2022 Structural basis for modulation of human Na V 1.3 by clinical drug and selective antagonist. Nat Commun doi:10.1038/s41467-022-28808-5
2021 Structural Basis for Pore Blockade of the Human Cardiac Sodium Channel Na v 1.5 by the Antiarrhythmic Drug Quinidine*. Angew.Chem.Int.Ed.Engl. doi:10.1002/anie.202102196
2021 Structure of human Na v 1.5 reveals the fast inactivation-related segments as a mutational hotspot for the long QT syndrome. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2100069118
2021 Comparative structural analysis of human Na v 1.1 and Na v 1.5 reveals mutational hotspots for sodium channelopathies. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.2100066118
2021 Structural basis for voltage-sensor trapping of the cardiac sodium channel by a deathstalker scorpion toxin. Nat Commun doi:10.1038/s41467-020-20078-3
2021 Open-state structure and pore gating mechanism of the cardiac sodium channel. Cell doi:10.1016/j.cell.2021.08.021
2021 Structural Basis for High-Affinity Trapping of the Na V 1.7 Channel in Its Resting State by Tarantula Toxin. Mol.Cell doi:10.1016/j.molcel.2020.10.039
2020 Employing NaChBac for cryo-EM analysis of toxin action on voltage-gated Na + channels in nanodisc. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.1922903117
2020 Structure of the Cardiac Sodium Channel. Cell doi:10.1016/j.cell.2019.11.041
2019 Ca2+-dependent regulation of sodium channels NaV1.4 and NaV1.5 is controlled by the post-IQ motif. Nat Commun doi:10.1038/s41467-019-09570-7
2019 Crystal structures of Ca2+-calmodulin bound to NaVC-terminal regions suggest role for EF-hand domain in binding and inactivation. Proc.Natl.Acad.Sci.USA doi:10.1073/pnas.1818618116
2019 Molecular basis for pore blockade of human Na+channel Nav1.2 by the mu-conotoxin KIIIA. Science doi:10.1126/science.aaw2999
2019 Structures of human Nav1.7 channel in complex with auxiliary subunits and animal toxins. Science doi:10.1126/science.aaw2493
2019 Cryo-EM structures of a human-cockroach hybrid Nav channel in the presence and absence of the alpha-scorpion toxin AaH2. Science
2019 Structural basis of alpha-scorpion toxin action on Na v channels. Science doi:10.1126/science.aav8573
2019 Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin. Cell doi:10.1016/j.cell.2018.12.018
2018 Structural basis for the modulation of voltage-gated sodium channels by animal toxins. Science doi:10.1126/science.aau2596
2018 Structure of the human voltage-gated sodium channel Nav1.4 in complex with beta 1. Science doi:10.1126/science.aau2486