Cryo-EM structure of full-length Nup188. Determined by electron microscopy at 2.81 Å resolution. Released 30 Mar 2022.
Explore 7WO9 in 3D Show helices and sheets RCSB PDB PDBe
7WO9 contains 96 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 | 15-24 | 10 | |
| α-helix | 29-31 | 3 | |
| α-helix | 34-46 | 13 | |
| α-helix | 70-79 | 10 | |
| α-helix | 87-91 | 5 | |
| α-helix | 95-118 | 24 | |
| α-helix | 120-122 | 3 | |
| α-helix | 124-131 | 8 | |
| α-helix | 134-150 | 17 | |
| α-helix | 156-161 | 6 | |
| α-helix | 168-198 | 31 | |
| α-helix | 206-215 | 10 | |
| α-helix | 216-220 | 5 | |
| α-helix | 221-228 | 8 | |
| α-helix | 248-272 | 25 | |
| β-strand | 275-276 | 2 | 1 |
| β-strand | 281-282 | 2 | 1 |
| α-helix | 287-290 | 4 | |
| α-helix | 294-307 | 14 | |
| α-helix | 319-335 | 17 | |
| α-helix | 346-355 | 10 | |
| α-helix | 358-368 | 11 | |
| α-helix | 373-386 | 14 | |
| α-helix | 387-389 | 3 | |
| α-helix | 394-404 | 11 | |
| α-helix | 409-416 | 8 | |
| α-helix | 419-430 | 12 | |
| α-helix | 439-445 | 7 | |
| α-helix | 450-458 | 9 | |
| β-strand | 460-466 | 7 | 2 |
| α-helix | 470-472 | 3 | |
| β-strand | 475-476 | 2 | 2 |
| β-strand | 496-499 | 4 | 2 |
| β-strand | 503-505 | 3 | 3 |
| α-helix | 506-507 | 2 | |
| β-strand | 518-520 | 3 | 3 |
| β-strand | 525-529 | 5 | 2 |
| β-strand | 552-559 | 8 | 2 |
| α-helix | 561-578 | 18 | |
| α-helix | 585-601 | 17 | |
| α-helix | 608-618 | 11 | |
| α-helix | 634-648 | 15 | |
| α-helix | 651-664 | 14 | |
| α-helix | 669-678 | 10 | |
| α-helix | 690-694 | 5 | |
| α-helix | 695-699 | 5 | |
| α-helix | 700-702 | 3 | |
| α-helix | 706-722 | 17 | |
| α-helix | 732-750 | 19 | |
| α-helix | 753-755 | 3 | |
| α-helix | 761-783 | 23 | |
| β-strand | 785 | 1 | 4 |
| α-helix | 796-806 | 11 | |
| α-helix | 815-824 | 10 | |
| α-helix | 826-828 | 3 | |
| α-helix | 830-835 | 6 | |
| α-helix | 843-863 | 21 | |
| α-helix | 869-871 | 3 | |
| α-helix | 872-879 | 8 | |
| α-helix | 882-888 | 7 | |
| α-helix | 897-909 | 13 | |
| α-helix | 919-923 | 5 | |
| α-helix | 925-939 | 15 | |
| α-helix | 946-961 | 16 | |
| α-helix | 965-973 | 9 | |
| α-helix | 980-982 | 3 | |
| α-helix | 990-992 | 3 | |
| α-helix | 994-1002 | 9 | |
| α-helix | 1010-1022 | 13 | |
| α-helix | 1023-1027 | 5 | |
| α-helix | 1038-1049 | 12 | |
| α-helix | 1051-1053 | 3 | |
| α-helix | 1062-1088 | 27 | |
| α-helix | 1094-1100 | 7 | |
| α-helix | 1105-1109 | 5 | |
| α-helix | 1110-1113 | 4 | |
| α-helix | 1120-1133 | 14 | |
| α-helix | 1139-1142 | 4 | |
| β-strand | 1143 | 1 | 5 |
| β-strand | 1144 | 1 | 4 |
| β-strand | 1158 | 1 | 5 |
| α-helix | 1160-1166 | 7 | |
| α-helix | 1171-1174 | 4 | |
| α-helix | 1183-1217 | 35 | |
| α-helix | 1221-1222 | 2 | |
| α-helix | 1224-1238 | 15 | |
| α-helix | 1249-1267 | 19 | |
| α-helix | 1274-1288 | 15 | |
| α-helix | 1299-1303 | 5 | |
| α-helix | 1305-1307 | 3 | |
| α-helix | 1309-1318 | 10 | |
| α-helix | 1329-1359 | 31 | |
| α-helix | 1380-1383 | 4 | |
| α-helix | 1388-1396 | 9 | |
| α-helix | 1402-1415 | 14 | |
| α-helix | 1419-1430 | 12 | |
| β-strand | 1433 | 1 | 6 |
| β-strand | 1436 | 1 | 6 |
| α-helix | 1440-1451 | 12 | |
| α-helix | 1454-1461 | 8 | |
| α-helix | 1465-1470 | 6 | |
| α-helix | 1473-1479 | 7 | |
| α-helix | 1489-1509 | 21 | |
| α-helix | 1515-1524 | 10 | |
| α-helix | 1526-1538 | 13 | |
| α-helix | 1545-1557 | 13 | |
| α-helix | 1560-1563 | 4 | |
| α-helix | 1592-1605 | 14 | |
| α-helix | 1609-1615 | 7 | |
| α-helix | 1621-1628 | 8 | |
| α-helix | 1633-1654 | 22 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nucleoporin NUP188 | A | protein | 1655 | Saccharomyces cerevisiae S288C | P52593 (AlphaFold model) |
>7WO9_1 Nucleoporin NUP188 (chains A) MATPSFGNSSPQLTFTHVANFMNDAAADVSAVDAKQLAQIRQFLKANKTNLIESLNTIRQ NVTSSGDHNKLRSTIANLLQINVDNDPFFAQSEDLSHAVEFFMSERSSRLHIVYSLLVNP DIDLETYSFIDNDRFNVVGKLISIISSVIQNYDIITASSLAHDYNNDQDMFTIVSLVQLK KFSDLKFILQILQILNLMILNTKVPVDIVNQWFLQYQNQFVEFCRNINSTDKSIDTSSLQ LYKFQNFQDLSYLSETLISRISSLFTITTILILGLNTSIAQFDIQSPLYMDTETFDTVNS ALENDVATNIVNEDPIFHPMIHYSWSFILYYRRALQSSESFDDSDITKFALFAESHDVLQ KLNTLSEILSFDPVYTTVITVFLEFSLNFIPITASTSRVFAKIISKAPEQFIENFLTNDT FEKKLSIIKAKLPLLNESLIPLINLALIDTEFANFELKDICSFAVTKSSLNDLDYDLIAD TITNSSSSSDIIVPDLIELKSDLLVAPPLENENSNCLLSIPKSTKGKILTIKQQQQQQQQ QNGQQPPTTSNLIIFLYKFNGWSLVGRILQNLLHSYMEKGTQLDDLQHELMISIIKLVTN VVDPKTSIEKSSEILSYLSNSLDTSASTINGASIIQVIFEIFEISLQRKDYTSIVQCCEF MTMLTPNYLHLVSSYLNKSDLLDKYGKTGLSNMILGSVELSTGDYTFTIQLLKLTKVFIR ESLSLKNIHISKRSKIDIINKLILHAIHIFESYYNWKYNNFLQKFEIAFHLTLIFYDVLH DVFTINPHQKDQLIISSSANKLLQLFLTPMDSIDLAPNTLTNILISPLNTTTKILGDKIL GNLYSKVMNNSFKLCTLLIAIRGSNRDLKPSNLEKLLFINSSKLVDVYTLPSYVHFKVQI IELLSYLVEAPWNDDYPFLLSFLGEAKSMAFLKEVLSDLSSPVQDWNLLRSLYIFFTTLL ESKQDGLSILFLTGQFASNKKINDESSIDKKSSILTVLQKNSLLLDSTPEEVSCKLLETI TYVLNTWTNSKIFIKDPKFVNSLLAKLKDSKKLFQKKENLTRDETVSLIKKYKLISRIVE IFALCIYNSTDSNSEILNFLNQEDLFELVHHFFQIDGFNKTFHDELNLKFKEKWPSLELQ SFQKIPLSRINENENFGYDIPLLDIVLKADRSWNEPSKSQTNFKEEITDASLNLQYVNYE ISTAKAWGALITTFVKRSTVPLNDGFVDLVEHFLKLNIDFGSDKQMFTQIYLERIELSFY ILYSFKLSGKLLKEEKIIELMNKIFTIFKSGEIDFIKNIGKSLKNNFYRPLLRSVLVLLE LVSSGDRFIELISDQLLEFFELVFSKGVYLILSEILCQINKCSTRGLSTDHTTQIVNLED NTQDLLLLLSLFKKITNVNPSKNFNVILASSLNEVGTLKVILNLYSSAHLIRINDEPILG QITLTFISELCSIEPIAAKLINSGLYSVLLESPLSVAIQQGDIKPEFSPRLHNIWSNGLL SIVLLLLSQFGIKVLPETCLFVSYFGKQIKSTIYNWGDNKLAVSSSLIKETNQLVLLQKM LNLLNYQELFIQPKNSDDQQEAVELVIGLDSEHDKKRLSAALSKFLTHPKYLNSRIIPTT LEEQQQLEDESSRLEFVKGISRDIKALQDSLFKDV
Near-atomic structure of the inner ring of the Saccharomyces cerevisiae nuclear pore complex. Li, Z., Chen, S., Zhao, L. et al. Cell Res (2022) 32:437-450. DOI 10.1038/s41422-022-00632-y · PubMed
Other PDB entries of the same protein (UniProt P52593 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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