Cryo-EM structure of apo human separase with the mutation C2029S. Determined by electron microscopy at 3.1 Å resolution. Released 3 Sept 2025.
Explore 9HM7 in 3D Show helices and sheets RCSB PDB PDBe
9HM7 contains 70 α-helices and 17 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 | 423-441 | 19 | |
| α-helix | 447-469 | 23 | |
| α-helix | 473-490 | 18 | |
| α-helix | 502-516 | 15 | |
| α-helix | 521-533 | 13 | |
| α-helix | 544-559 | 16 | |
| α-helix | 562-566 | 5 | |
| α-helix | 569-573 | 5 | |
| α-helix | 578-594 | 17 | |
| α-helix | 600-613 | 14 | |
| α-helix | 619-638 | 20 | |
| α-helix | 642-645 | 4 | |
| α-helix | 649-661 | 13 | |
| α-helix | 670-673 | 4 | |
| α-helix | 677-703 | 27 | |
| α-helix | 711-714 | 4 | |
| α-helix | 719-723 | 5 | |
| α-helix | 739-759 | 21 | |
| α-helix | 763-764 | 2 | |
| α-helix | 769-785 | 17 | |
| α-helix | 789-806 | 18 | |
| α-helix | 809-825 | 17 | |
| α-helix | 829-843 | 15 | |
| α-helix | 851-870 | 20 | |
| α-helix | 874-885 | 12 | |
| α-helix | 888-891 | 4 | |
| α-helix | 895-912 | 18 | |
| α-helix | 916-918 | 3 | |
| α-helix | 921-928 | 8 | |
| α-helix | 935-953 | 19 | |
| α-helix | 975-1001 | 27 | |
| α-helix | 1004-1021 | 18 | |
| α-helix | 1024-1040 | 17 | |
| α-helix | 1044-1061 | 18 | |
| α-helix | 1154-1173 | 20 | |
| α-helix | 1180-1206 | 27 | |
| α-helix | 1215-1216 | 2 | |
| α-helix | 1220-1236 | 17 | |
| α-helix | 1242-1255 | 14 | |
| α-helix | 1262-1277 | 16 | |
| α-helix | 1286-1291 | 6 | |
| α-helix | 1481-1484 | 4 | |
| α-helix | 1573-1588 | 16 | |
| α-helix | 1594-1608 | 15 | |
| α-helix | 1609-1611 | 3 | |
| α-helix | 1613-1621 | 9 | |
| 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 |
| β-strand | 1737-1742 | 6 | 1 |
| α-helix | 1750-1767 | 18 | |
| α-helix | 1773-1793 | 21 | |
| α-helix | 1794-1799 | 6 | |
| α-helix | 1800-1806 | 7 | |
| α-helix | 1814-1829 | 16 | |
| α-helix | 1836-1844 | 9 | |
| α-helix | 1846-1848 | 3 | |
| α-helix | 1851-1861 | 11 | |
| α-helix | 1866-1880 | 15 | |
| β-strand | 1890-1895 | 6 | 1 |
| α-helix | 1904-1906 | 3 | |
| β-strand | 1915-1917 | 3 | 1 |
| α-helix | 1921-1932 | 12 | |
| α-helix | 1937-1940 | 4 | |
| β-strand | 1943 | 1 | 2 |
| β-strand | 1948-1952 | 5 | 1 |
| α-helix | 1959-1971 | 13 | |
| β-strand | 1975-1979 | 5 | 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 | 2045-2051 | 7 | |
| β-strand | 2056-2060 | 5 | 1 |
| α-helix | 2066-2081 | 16 | |
| β-strand | 2088 | 1 | 4 |
| α-helix | 2089-2096 | 8 | |
| β-strand | 2110-2114 | 5 | 1 |
| β-strand | 2118 | 1 | 4 |
| β-strand | 2119 | 1 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Separin | A | protein | 2217 | Homo sapiens | Q14674 (AlphaFold model) |
>9HM7_1 Separin (chains A) MSGDYKDHDGDYKDHDIDYKDDDDKSGPGGSGGSGGGSGGGSGENLYFQGGGSGGSGMRS FKRVNFGTLLSSQKEAEELLPDLKEFLSNPPAGFPSSRSDAERRQACDAILRACNQQLTA KLACPRHLGSLLELAELACDGYLVSTPQRPPLYLERILFVLLRNAAAQGSPEVTLRLAQP LHACLVQCSREAAPQDYEAVARGSFSLLWKGAEALLERRAAFAARLKALSFLVLLEDEST PCEVPHFASPTACRAVAAHQLFDASGHGLNEADADFLDDLLSRHVIRALVGERGSSSGLL SPQRALCLLELTLEHCRRFCWSRHHDKAISAVEKAHSYLRNTNLAPSLQLCQLGVKLLQV GEEGPQAVAKLLIKASAVLSKSMEAPSPPLRALYESCQFFLSGLERGTKRRYRLDAILSL FAFLGGYCSLLQQLRDDGVYGGSSKQQQSFLQMYFQGLHLYTVVVYDFAQGCQIVDLADL TQLVDSCKSTVVWMLEALEGLSGQELTDHMGMTASYTSNLAYSFYSHKLYAEACAISEPL CQHLGLVKPGTYPEVPPEKLHRCFRLQVESLKKLGKQAQGCKMVILWLAALQPCSPEHMA EPVTFWVRVKMDAARAGDKELQLKTLRDSLSGWDPETLALLLREELQAYKAVRADTGQER FNIICDLLELSPEETPAGAWARATHLVELAQVLCYHDFTQQTNCSALDAIREALQLLDSV RPEAQARDQLLDDKAQALLWLYICTLEAKMQEGIERDRRAQAPGNLEEFEVNDLNYEDKL QEDRFLYSNIAFNLAADAAQSKCLDQALALWKELLTKGQAPAVRCLQQTAASLQILAALY QLVAKPMQALEVLLLLRIVSERLKDHSKAAGSSCHITQLLLTLGCPSYAQLHLEEAASSL KHLDQTTDTYLLLSLTCDLLRSQLYWTHQKVTKGVSLLLSVLRDPALQKSSKAWYLLRVQ VLQLVAAYLSLPSNNLSHSLWEQLCAQGWQTPEIALIDSHKLLRSIILLLMGSDILSTQK AAVETSFLDYGENLVQKWQVLSEVLSCSEKLVCHLGRLGSVSEAKAFCLEALKLTTKLQI PRQCALFLVLKGELELARNDIDLCQSDLQQVLFLLESCTEFGGVTQHLDSVKKVHLQKGK QQAQVPCPPQLPEEELFLRGPALELVATVAKEPGPIAPSTNSSPVLKTKPQPIPNFLSHS PTCDCSLCASPVLTAVCLRWVLVTAGVRLAMGHQAQGLDLLQVVLKGCPEAAERLTQALQ ASLNHKTPPSLVPSLLDEILAQAYTLLALEGLNQPSNESLQKVLQSGLKFVAARIPHLEP WRASLLLIWALTKLGGLSCCTTQLFASSWGWQPPLIKSVPGSEPSKTQGQKRSGRGRQKL ASAPLSLNNTSQKGLEGRGLPCTPKPPDRIRQAGPHVPFTVFEEVCPTESKPEVPQAPRV QQRVQTRLKVNFSDDSDLEDPVSAEAWLAEEPKRRGTASRGRGRARKGLSLKTDAVVAPG SAPGNPGLNGRSRRAKKVASRHCEERRPQRASDQARPGPEIMRTIPEEELTDNWRKMSFE ILRGSDGEDSASGGKTPAPGPEAASGEWELLRLDSSKKKLPSPCPDKESDKDLGPRLQLP SAPVATGLSTLDSICDSLSVAFRGISHCPPSGLYAHLCRFLALCLGHRDPYATAFLVTES VSITCRHQLLTHLHRQLSKAQKHRGSLEIADQLQGLSLQEMPGDVPLARIQRLFSFRALE SGHFPQPEKESFQERLALIPSGVTVCVLALATLQPGTVGNTLLLTRLEKDSPPVSVQIPT GQNKLHLRSVLNEFDAIQKAQKENSSCTDKREWWTGRLALDHRMEVLIASLEKSVLGCWK GLLLPSSEEPGPAQEASRLQELLQDCGWKYPDRTLLKIMLSGAGALTPQDIQALAYGLCP TQPERAQELLNEAVGRLQGLTVPSNSHLVLVLDKDLQKLPWESMPSLQALPVTRLPSFRF LLSYSIIKEYGASPVLSQGVDPRSTFYVLNPHNNLSSTEEQFRANFSSEAGWRGVVGEVP RPEQVQEALTKHDLYIYAGHGAGARFLDGQAVLRLSCRAVALLFGSSSAALAVHGNLEGA GIVLKYIMAGCPLFLGNLWDVTDRDIDRYTEALLQGWLGAGPGAPLLYYVNQARQAPRLK YLIGAAPIAYGLPVSLRSSLAEENLYFQSWSHPQFEKGGGSGGGSGGGSWSHPQFEK
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 1 |
Substrate recognition by human separase. Yu, J., Schmidt, S., Botto, M. et al. Sci Adv (2025) 11:eady9807-eady9807. DOI 10.1126/sciadv.ady9807 · PubMed
Other PDB entries of the same protein (UniProt Q14674 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9HM7 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.