Structure of human Nav1.7 in complex with PF-05089771. Determined by electron microscopy at 2.7 Å resolution. Released 14 Jun 2023.
Explore 8I5G in 3D Show helices and sheets RCSB PDB PDBe
8I5G contains 80 α-helices and 43 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 14 | 1 | 8 |
| α-helix | 17-33 | 17 | |
| β-strand | 58 | 1 | 9 |
| α-helix | 59-60 | 2 | |
| α-helix | 61-63 | 3 | |
| α-helix | 65-67 | 3 | |
| β-strand | 75 | 1 | 8 |
| β-strand | 87-91 | 5 | 8 |
| β-strand | 96 | 1 | 9 |
| β-strand | 97-101 | 5 | 8 |
| β-strand | 105 | 1 | 10 |
| β-strand | 109 | 1 | 10 |
| α-helix | 114-123 | 10 | |
| α-helix | 126-143 | 18 | |
| α-helix | 152-174 | 23 | |
| α-helix | 187-205 | 19 | |
| α-helix | 210-216 | 7 | |
| α-helix | 217-224 | 8 | |
| α-helix | 231-243 | 13 | |
| α-helix | 246-267 | 22 | |
| α-helix | 270-272 | 3 | |
| β-strand | 273-277 | 5 | 11 |
| α-helix | 286-290 | 5 | |
| α-helix | 296-299 | 4 | |
| β-strand | 303 | 1 | 11 |
| α-helix | 312-314 | 3 | |
| α-helix | 324-325 | 2 | |
| β-strand | 328-332 | 5 | 11 |
| α-helix | 335-336 | 2 | |
| α-helix | 338-340 | 3 | |
| α-helix | 347-359 | 13 | |
| α-helix | 363-374 | 12 | |
| α-helix | 376-378 | 3 | |
| α-helix | 379-385 | 7 | |
| α-helix | 386-393 | 8 | |
| α-helix | 394-417 | 24 | |
| α-helix | 729-740 | 12 | |
| α-helix | 743-747 | 5 | |
| α-helix | 748-760 | 13 | |
| α-helix | 761-763 | 3 | |
| α-helix | 770-797 | 28 | |
| α-helix | 800-803 | 4 | |
| α-helix | 807-824 | 18 | |
| α-helix | 834-847 | 14 | |
| α-helix | 850-863 | 14 | |
| α-helix | 867-894 | 28 | |
| α-helix | 896-898 | 3 | |
| α-helix | 913-925 | 13 | |
| α-helix | 929-939 | 11 | |
| α-helix | 941-968 | 28 | |
| α-helix | 969-973 | 5 | |
| α-helix | 987-1013 | 27 | |
| α-helix | 1176-1189 | 14 | |
| α-helix | 1192-1207 | 16 | |
| α-helix | 1208-1211 | 4 | |
| α-helix | 1216-1218 | 3 | |
| α-helix | 1220-1255 | 36 | |
| α-helix | 1257-1277 | 21 | |
| α-helix | 1284-1290 | 7 | |
| α-helix | 1291-1299 | 9 | |
| α-helix | 1300-1303 | 4 | |
| α-helix | 1305-1343 | 39 | |
| β-strand | 1349-1352 | 4 | 12 |
| β-strand | 1357-1358 | 2 | 12 |
| α-helix | 1359-1360 | 2 | |
| β-strand | 1366 | 1 | 13 |
| α-helix | 1367-1376 | 10 | |
| β-strand | 1380-1383 | 4 | 12 |
| α-helix | 1392-1404 | 13 | |
| α-helix | 1408-1416 | 9 | |
| β-strand | 1423 | 1 | 13 |
| α-helix | 1431-1433 | 3 | |
| α-helix | 1434-1441 | 8 | |
| α-helix | 1442-1447 | 6 | |
| α-helix | 1448-1466 | 19 | |
| α-helix | 1476-1488 | 13 | |
| 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 | 1577-1602 | 26 | |
| α-helix | 1606-1612 | 7 | |
| α-helix | 1613-1616 | 4 | |
| α-helix | 1617-1620 | 4 | |
| α-helix | 1621-1625 | 5 | |
| α-helix | 1628-1665 | 38 | |
| α-helix | 1684-1695 | 12 | |
| α-helix | 1700-1707 | 8 | |
| β-strand | 1720 | 1 | 14 |
| β-strand | 1727 | 1 | 14 |
| α-helix | 1733-1766 | 34 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 25-27 | 3 | |
| β-strand | 29-31 | 3 | 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 | 132-144 | 13 | 4 |
| β-strand | 145-147 | 3 | 1 |
| α-helix | 151-153 | 3 | |
| α-helix | 154-191 | 38 |
| 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 |
| β-strand | 64-70 | 7 | 6 |
| β-strand | 78-83 | 6 | 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 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium channel subunit beta-1 | B | protein | 192 | Homo sapiens | Q07699 (AlphaFold model) |
| Sodium channel subunit beta-2 | C | protein | 215 | Homo sapiens | O60939 (AlphaFold model) |
| Sodium channel protein type 9 subunit alpha | A | protein | 1988 | Homo sapiens | Q15858 (AlphaFold model) |
>8I5G_1 Sodium channel subunit beta-1 (chains B) MGRLLALVVGAALVSSACGGCVEVDSETEAVYGMTFKILCISCKRRSETNAETFTEWTFR QKGTEEFVKILRYENEVLQLEEDERFEGRVVWNGSRGTKDLQDLSIFITNVTYNHSGDYE CHVYRLLFFENYEHNTSVVKKIHIEVVDKANRDMASIVSEIMMYVLIVVLTIWLVAEMIY CYKKIAAATETA
>8I5G_2 Sodium channel subunit beta-2 (chains C) MHRDAWLPRPAFSLTGLSLFFSLVPPGRSMEVTVPATLNVLNGSDARLPCTFNSCYTVNH KQFSLNWTYQECNNCSEEMFLQFRMKIINLKLERFQDRVEFSGNPSKYDVSVMLRNVQPE DEGIYNCYIMNPPDRHRGHGKIHLQVLMEEPPERDSTVAVIVGASVGGFLAVVILVLMVV KCVRRKKEQKLSTDDLKTEEEGKTDGEGNPDDGAK
>8I5G_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
| ID | Name | Formula | Copies |
|---|---|---|---|
| Y01 | Cholesterol hemisuccinate | C31 H50 O4 | 2 |
| 9Z9 | (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en | C34 H56 O5 | 1 |
| LPE | 1-O-octadecyl-sn-glycero-3-phosphocholine | C26 H57 N O6 P | 8 |
| PCW | 1,2-dioleoyl-sn-glycero-3-phosphocholine | C44 H85 N O8 P | 5 |
| T70 | PF-05089771 | C18 H12 Cl2 F N5 O3 S2 | 1 |
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 5 |
Water and common crystallization additives (NA) are not listed.
Structural mapping of Na v 1.7 antagonists. Wu, Q., Huang, J., Fan, X. et al. Nat Commun (2023) 14:3224-3224. DOI 10.1038/s41467-023-38942-3 · PubMed
Other PDB entries of the same protein (UniProt Q07699 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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