CryoEM structure of the human Separase-Securin complex. Determined by electron microscopy at 2.9 Å resolution. Released 4 Aug 2021.
Explore 7NJ1 in 3D Show helices and sheets RCSB PDB PDBe
7NJ1 contains 76 α-helices and 18 β-strands across 2 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 |
|---|---|---|---|
| α-helix | 245-264 | 20 | |
| α-helix | 269-281 | 13 | |
| α-helix | 287-303 | 17 | |
| α-helix | 309-325 | 17 | |
| α-helix | 332-348 | 17 | |
| α-helix | 357-379 | 23 | |
| α-helix | 381-385 | 5 | |
| α-helix | 387-414 | 28 | |
| α-helix | 420-440 | 21 | |
| α-helix | 446-468 | 23 | |
| α-helix | 473-489 | 17 | |
| α-helix | 500-516 | 17 | |
| α-helix | 520-533 | 14 | |
| α-helix | 543-558 | 16 | |
| α-helix | 562-566 | 5 | |
| α-helix | 569-572 | 4 | |
| α-helix | 578-594 | 17 | |
| α-helix | 600-613 | 14 | |
| α-helix | 619-636 | 18 | |
| α-helix | 649-662 | 14 | |
| α-helix | 670-701 | 32 | |
| α-helix | 729-736 | 8 | |
| α-helix | 740-758 | 19 | |
| α-helix | 769-785 | 17 | |
| α-helix | 789-805 | 17 | |
| α-helix | 809-825 | 17 | |
| α-helix | 830-844 | 15 | |
| α-helix | 851-870 | 20 | |
| α-helix | 874-885 | 12 | |
| α-helix | 888-891 | 4 | |
| α-helix | 895-912 | 18 | |
| α-helix | 921-928 | 8 | |
| α-helix | 935-953 | 19 | |
| α-helix | 976-1000 | 25 | |
| α-helix | 1004-1021 | 18 | |
| α-helix | 1024-1040 | 17 | |
| α-helix | 1044-1061 | 18 | |
| α-helix | 1148-1152 | 5 | |
| α-helix | 1154-1173 | 20 | |
| α-helix | 1178-1206 | 29 | |
| α-helix | 1218-1231 | 14 | |
| α-helix | 1233-1236 | 4 | |
| α-helix | 1247-1256 | 10 | |
| α-helix | 1263-1277 | 15 | |
| α-helix | 1574-1588 | 15 | |
| α-helix | 1595-1607 | 13 | |
| α-helix | 1613-1622 | 10 | |
| α-helix | 1626-1646 | 21 | |
| α-helix | 1668-1677 | 10 | |
| α-helix | 1689-1700 | 12 | |
| α-helix | 1702-1703 | 2 | |
| β-strand | 1706-1714 | 9 | 1 |
| β-strand | 1724-1730 | 7 | 1 |
| α-helix | 1735-1736 | 2 | |
| β-strand | 1737-1742 | 6 | 1 |
| α-helix | 1751-1767 | 17 | |
| α-helix | 1773-1793 | 21 | |
| α-helix | 1794-1799 | 6 | |
| α-helix | 1804-1806 | 3 | |
| α-helix | 1815-1829 | 15 | |
| α-helix | 1837-1842 | 6 | |
| α-helix | 1846-1848 | 3 | |
| α-helix | 1851-1861 | 11 | |
| α-helix | 1867-1879 | 13 | |
| β-strand | 1890-1894 | 5 | 1 |
| α-helix | 1904-1906 | 3 | |
| β-strand | 1915-1917 | 3 | 1 |
| α-helix | 1921-1933 | 13 | |
| α-helix | 1937-1940 | 4 | |
| β-strand | 1943 | 1 | 2 |
| β-strand | 1948-1952 | 5 | 1 |
| α-helix | 1959-1971 | 13 | |
| β-strand | 1975 | 1 | 1 |
| β-strand | 1978-1979 | 2 | 1 |
| α-helix | 1982-1984 | 3 | |
| α-helix | 1985-1994 | 10 | |
| β-strand | 1997-2001 | 5 | 1 |
| α-helix | 2012-2016 | 5 | |
| β-strand | 2023-2027 | 5 | 1 |
| β-strand | 2035 | 1 | 3 |
| α-helix | 2041-2042 | 2 | |
| β-strand | 2043 | 1 | 3 |
| α-helix | 2045-2050 | 6 | |
| β-strand | 2056-2059 | 4 | 1 |
| α-helix | 2067-2083 | 17 | |
| β-strand | 2088 | 1 | 4 |
| α-helix | 2089-2095 | 7 | |
| α-helix | 2096-2098 | 3 | |
| β-strand | 2111-2114 | 4 | 1 |
| β-strand | 2118 | 1 | 4 |
| β-strand | 2119 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 112-116 | 5 | |
| α-helix | 122-125 | 4 | |
| α-helix | 155-157 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Separin | A | protein | 2160 | Homo sapiens | Q14674 (AlphaFold model) |
| Securin | B | protein | 202 | Homo sapiens | O95997 (AlphaFold model) |
>7NJ1_1 Separin (chains A) MRSFKRVNFGTLLSSQKEAEELLPDLKEFLSNPPAGFPSSRSDAERRQACDAILRACNQQ LTAKLACPRHLGSLLELAELACDGYLVSTPQRPPLYLERILFVLLRNAAAQGSPEVTLRL AQPLHACLVQCSREAAPQDYEAVARGSFSLLWKGAEALLERRAAFAARLKALSFLVLLED ESTPCEVPHFASPTACRAVAAHQLFDASGHGLNEADADFLDDLLSRHVIRALVGERGSSS GLLSPQRALCLLELTLEHCRRFCWSRHHDKAISAVEKAHSYLRNTNLAPSLQLCQLGVKL LQVGEEGPQAVAKLLIKASAVLSKSMEAPSPPLRALYESCQFFLSGLERGTKRRYRLDAI LSLFAFLGGYCSLLQQLRDDGVYGGSSKQQQSFLQMYFQGLHLYTVVVYDFAQGCQIVDL ADLTQLVDSCKSTVVWMLEALEGLSGQELTDHMGMTASYTSNLAYSFYSHKLYAEACAIS EPLCQHLGLVKPGTYPEVPPEKLHRCFRLQVESLKKLGKQAQGCKMVILWLAALQPCSPE HMAEPVTFWVRVKMDAARAGDKELQLKTLRDSLSGWDPETLALLLREELQAYKAVRADTG QERFNIICDLLELSPEETPAGAWARATHLVELAQVLCYHDFTQQTNCSALDAIREALQLL DSVRPEAQARDQLLDDKAQALLWLYICTLEAKIQEGIERDRRAQAPGNLEEFEVNDLNYE DKLQEDRFLYSNIAFNLAADAAQSKCLDQALALWKELLTKGQAPAVRCLQQTAASLQILA ALYQLVAKPMQALEVLLLLRIVSERLKDHSKAAGSSCHITQLLLTLGCPSYAQLHLEEAA SSLKHLDQTTDTYLLLSLTCDLLRSQLYWTHQKVTKGVSLLLSVLRDPALQKSSKAWYLL RVQVLQLVAAYLSLPSNNLSHSLWEQLCAQGWQTPEIALIDSHKLLRSIILLLMGSDILS TQKAAVETSFLDYGENLVQKWQVLSEVLSCSEKLVCHLGRLGSVSEAKAFCLEALKLTTK LQIPRQCALFLVLKGELELARNDIDLCQSDLQQVLFLLESCTEFGGVTQHLDSVKKVHLQ KGKQQAQVPCPPQLPEEELFLRGPALELVATVAKEPGPIAPSTNSSPVLKTKPQPIPNFL SHSPTCDCSLCASPVLTAVCLRWVLVTAGVRLAMGHQAQGLDLLQVVLKGCPEAAERLTQ ALQASLNHKTPPSLVPSLLDEILAQAYTLLALEGLNQPSNESLQKVLQSGLKFVAARIPH LEPWRASLLLIWALTKLGGLSCCTTQLFASSWGWQPPLIKSVPGSEPSKTQGQKRSGRGR QKLASAPLSLNNTSQKGLEGRGLPCTPKPPDRIRQAGPHVPFTVFEEVCPTESKPEVPQA PRVQQRVQTRLKVNFSDDSDLEDPVSAEAWLAEEPKRRGTASRGRGRARKGLSLKTDAVV APGSAPGNPGLNGRSRRAKKVASRHCEERRPQRASDQARPGPEIMRTIPEEELTDNWRKM SFEILRGSDGEDSASGGKTPAPGPEAASGEWELLRLDSSKKKLPSPCPDKESDKDLGPRL QLPSAPVATGLSTLDSICDSLSVAFRGISHCPPSGLYAHLCRFLALCLGHRDPYATAFLV TESVSITCRHQLLTHLHRQLSKAQKHRGSLEIADQLQGLSLQEMPGDVPLARIQRLFSFR ALESGHFPQPEKESFQERLALIPSGVTVCVLALATLQPGTVGNTLLLTRLEKDSPPVSVQ IPTGQNKLHLRSVLNEFDAIQKAQKENSSCTDKREWWTGRLALDHRMEVLIASLEKSVLG CWKGLLLPSSEEPGPAQEASRLQELLQDCGWKYPDRTLLKIMLSGAGALTPQDIQALAYG LCPTQPERAQELLNEAVGRLQGLTVPSNSHLVLVLDKDLQKLPWESMPSLQALPVTRLPS FRFLLSYSIIKEYGASPVLSQGVDPRSTFYVLNPHNNLSSTEEQFRANFSSEAGWRGVVG EVPRPEQVQEALTKHDLYIYAGHGAGARFLDGQAVLRLSCRAVALLFGCSSAALAVHGNL EGAGIVLKYIMAGCPLFLGNLWDVTDRDIDRYTEALLQGWLGAGPGAPLLYYVNQARQAP RLKYLIGAAPIAYGLPVSLRSSLAEENLYFQSWSHPQFEKGGGSGGGSGGGSWSHPQFEK
>7NJ1_2 Securin (chains B) MATLIYVDKENGEPGTRVVAKDGLKLGSGPSIKALDGRSQVSTPRFGKTFDAPPALPKAT RKALGTVNRATEKSVKTKGPLKQKQPSFSAKKMTEKTVKAKSSVPASDDAYPEIEKFFPF NPLDFESFDLPEEHQIAHLPLSGVPLMILDEERELEKLFQLGPPSPVKMPSPPWESNLLQ SPSSILSTLDVELPPVCCDIDI
Structural basis of human separase regulation by securin and CDK1-cyclin B1. Yu, J., Raia, P., Ghent, C.M. et al. Nature (2021) 596:138-142. DOI 10.1038/s41586-021-03764-0 · PubMed
Other PDB entries of the same protein (UniProt Q14674 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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