Nav1.5 in complex with TTX. Determined by electron microscopy at 3.4 Å resolution. Released 20 Aug 2025.
Explore 9ITH in 3D Show helices and sheets RCSB PDB PDBe
9ITH contains 66 α-helices and 15 β-strands across 1 chain. 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 121-129 | 9 | |
| α-helix | 131-148 | 18 | |
| α-helix | 160-179 | 20 | |
| α-helix | 193-209 | 17 | |
| α-helix | 219-227 | 9 | |
| α-helix | 229-232 | 4 | |
| α-helix | 234-249 | 16 | |
| α-helix | 252-271 | 20 | |
| β-strand | 279-282 | 4 | 1 |
| β-strand | 294-295 | 2 | 2 |
| β-strand | 301-302 | 2 | 2 |
| α-helix | 304-307 | 4 | |
| β-strand | 314 | 1 | 1 |
| β-strand | 316 | 1 | 3 |
| α-helix | 317 | 1 | |
| β-strand | 323 | 1 | 3 |
| β-strand | 339-342 | 4 | 1 |
| α-helix | 349-351 | 3 | |
| α-helix | 358-369 | 12 | |
| α-helix | 374-385 | 12 | |
| α-helix | 387-389 | 3 | |
| α-helix | 390-396 | 7 | |
| α-helix | 397-404 | 8 | |
| α-helix | 405-428 | 24 | |
| α-helix | 703-714 | 12 | |
| α-helix | 717-734 | 18 | |
| α-helix | 743-770 | 28 | |
| α-helix | 773-776 | 4 | |
| α-helix | 783-796 | 14 | |
| α-helix | 806-809 | 4 | |
| α-helix | 810-819 | 10 | |
| α-helix | 823-833 | 11 | |
| α-helix | 834-838 | 5 | |
| α-helix | 840-861 | 22 | |
| α-helix | 864-866 | 3 | |
| β-strand | 870 | 1 | 4 |
| β-strand | 875 | 1 | 4 |
| α-helix | 884-896 | 13 | |
| α-helix | 900-910 | 11 | |
| α-helix | 912-918 | 7 | |
| α-helix | 921-943 | 23 | |
| α-helix | 1191-1203 | 13 | |
| α-helix | 1205-1220 | 16 | |
| α-helix | 1221-1224 | 4 | |
| α-helix | 1233-1268 | 36 | |
| α-helix | 1272-1286 | 15 | |
| α-helix | 1287-1291 | 5 | |
| α-helix | 1299-1302 | 4 | |
| α-helix | 1303-1312 | 10 | |
| α-helix | 1313-1316 | 4 | |
| α-helix | 1318-1329 | 12 | |
| α-helix | 1331-1356 | 26 | |
| β-strand | 1361-1364 | 4 | 5 |
| α-helix | 1372-1374 | 3 | |
| β-strand | 1380 | 1 | 6 |
| α-helix | 1381-1384 | 4 | |
| β-strand | 1394-1397 | 4 | 5 |
| α-helix | 1405-1417 | 13 | |
| α-helix | 1421-1428 | 8 | |
| β-strand | 1436 | 1 | 6 |
| α-helix | 1444-1446 | 3 | |
| α-helix | 1447-1453 | 7 | |
| α-helix | 1454-1460 | 7 | |
| α-helix | 1461-1479 | 19 | |
| α-helix | 1489-1501 | 13 | |
| α-helix | 1522-1525 | 4 | |
| α-helix | 1528-1545 | 18 | |
| α-helix | 1554-1578 | 25 | |
| α-helix | 1587-1589 | 3 | |
| α-helix | 1592-1607 | 16 | |
| α-helix | 1608-1614 | 7 | |
| α-helix | 1618-1626 | 9 | |
| α-helix | 1627-1629 | 3 | |
| α-helix | 1630-1633 | 4 | |
| α-helix | 1634-1637 | 4 | |
| α-helix | 1641-1678 | 38 | |
| β-strand | 1689 | 1 | 7 |
| β-strand | 1692 | 1 | 7 |
| α-helix | 1697-1707 | 11 | |
| α-helix | 1713-1720 | 8 | |
| α-helix | 1745-1777 | 33 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium channel protein type 5 subunit alpha | A | protein | 2059 | Homo sapiens | Q14524 (AlphaFold model) |
>9ITH_1 Sodium channel protein type 5 subunit alpha (chains A) MASWSHPQFEKGGGARGGSGGGSWSHPQFEKGFDYKDDDDKGTMANFLLPRGTSSFRRFT RESLAAIEKRMAEKQARGSTTLQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPQELIG EPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPIRRAAVKILVHSLFNMLI MCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLD FSVIIMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLT VFCLSVFALIGLQLFMGNLRHKCVRNFTALNGTNGSVEADGLVWESLDLYLSDPENYLLK NGTSDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERL YQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEA MEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVNSHERRSKRRKRMSSGTEECGEDRLPKS DSEDGPRAMNHLSLTRGLSRTSMKPRSSRGSIFTFRRRDLGSEADFADDENSTAGESESH HTSLLVPWPLRRTSAQGQPSPGTSAPGHALHGKKNSTVDCNGVVSLLGAGDPEATSPGSH LLRPVMLEHPPDTTTPSEEPGGPQMLTSQAPCVDGFEEPGARQRALSAVSVLTSALEELE ESRHKCPPCWNRLAQRYLIWECCPLWMSIKQGVKLVVMDPFTDLTITMCIVLNTLFMALE HYNMTSEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELG LSRMSNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVG MQLFGKNYSELRDSDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLL VFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDREMNNLQLALARIQRGLRFVKRTT WDFCCGLLRQRPQKPAALAAQGQLPSCIATPYSPPPPETEKVPPTRKETRFEEGEQPGQG TPGDPEPVCVPIAVAESDTDDQEEDEENSLGTEEESSKQQESQPVSGGPEAPPDSRTWSQ VSATASSEAEASASQADWRQQWKAEPQAPGCGETPEDSCSEGSTADMTNTAELLEQIPDL GQDVKDPEDCFTEGCVRRCPCCAVDTTQAPGKVWWRLRKTCYHIVEHSWFETFIIFMILL SSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFL IVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNV LLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSQCESLNLTGELYWTK VKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEYNLYMYIYFVIFIIFG SFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKY QGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKINILAKINLLFVAIFTGECIV KLAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLI RGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQTF ANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPTLPNSNGSRGDCGSPAVGILFFTTYII ISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYSVLSDF ADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEE KFMAANPSKISYEPITTTLRRKHEEVSAMVIQRAFRRHLLQRSLKHASFLFRQQAGSGLS EEDAPEREGLIAYVMSENFSRPLGPPSSSSISSTSFPPSYDSVTRATSDNLQVRGSDYSH SEDLADFPPSPDRDRESIV
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 9 |
| 9SR | (1R,5R,6R,7R,9S,11S,12S,13S,14S)-3-amino-14-(hydroxymethyl)-8,10-dioxa-2,4-diaz… | C11 H17 N3 O8 | 1 |
| 9Z9 | (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en | C34 H56 O5 | 1 |
Critical role of extracellular loops in differential modulations of TTX-sensitive and TTX-resistant Na v channels. Wu, T., Yang, X., Jin, X. et al. Proc Natl Acad Sci U S A (2025) 122:e2510355122-e2510355122. DOI 10.1073/pnas.2510355122 · PubMed
Other PDB entries of the same protein (UniProt Q14524 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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