Cryo-EM structure of apo human separase. Determined by electron microscopy at 3.3 Å resolution. Released 3 Sept 2025.
Explore 9HMA in 3D Show helices and sheets RCSB PDB PDBe
9HMA contains 75 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 | 330-349 | 20 | |
| α-helix | 358-380 | 23 | |
| α-helix | 391-413 | 23 | |
| α-helix | 419-441 | 23 | |
| α-helix | 448-450 | 3 | |
| α-helix | 452-469 | 18 | |
| α-helix | 530-546 | 17 | |
| α-helix | 557-574 | 18 | |
| α-helix | 578-590 | 13 | |
| α-helix | 596-599 | 4 | |
| α-helix | 600-615 | 16 | |
| α-helix | 620-623 | 4 | |
| α-helix | 626-630 | 5 | |
| α-helix | 635-651 | 17 | |
| α-helix | 657-670 | 14 | |
| α-helix | 676-693 | 18 | |
| α-helix | 706-719 | 14 | |
| α-helix | 724-726 | 3 | |
| α-helix | 727-760 | 34 | |
| α-helix | 776-781 | 6 | |
| α-helix | 786-790 | 5 | |
| α-helix | 796-816 | 21 | |
| α-helix | 820-821 | 2 | |
| α-helix | 826-842 | 17 | |
| α-helix | 846-862 | 17 | |
| α-helix | 866-883 | 18 | |
| α-helix | 887-900 | 14 | |
| α-helix | 908-927 | 20 | |
| α-helix | 931-943 | 13 | |
| α-helix | 945-948 | 4 | |
| α-helix | 952-968 | 17 | |
| α-helix | 978-985 | 8 | |
| α-helix | 992-1011 | 20 | |
| α-helix | 1032-1058 | 27 | |
| α-helix | 1062-1078 | 17 | |
| α-helix | 1081-1097 | 17 | |
| α-helix | 1101-1118 | 18 | |
| α-helix | 1195-1198 | 4 | |
| α-helix | 1206-1209 | 4 | |
| α-helix | 1211-1230 | 20 | |
| α-helix | 1237-1263 | 27 | |
| α-helix | 1275-1293 | 19 | |
| α-helix | 1298-1300 | 3 | |
| α-helix | 1303-1313 | 11 | |
| α-helix | 1315-1317 | 3 | |
| α-helix | 1319-1334 | 16 | |
| α-helix | 1343-1345 | 3 | |
| α-helix | 1630-1645 | 16 | |
| α-helix | 1653-1665 | 13 | |
| α-helix | 1666-1668 | 3 | |
| α-helix | 1670-1678 | 9 | |
| α-helix | 1683-1700 | 18 | |
| α-helix | 1725-1734 | 10 | |
| α-helix | 1746-1756 | 11 | |
| α-helix | 1759-1760 | 2 | |
| β-strand | 1763-1771 | 9 | 1 |
| β-strand | 1781-1788 | 8 | 1 |
| β-strand | 1791-1799 | 9 | 1 |
| α-helix | 1807-1825 | 19 | |
| α-helix | 1830-1850 | 21 | |
| α-helix | 1851-1856 | 6 | |
| α-helix | 1857-1863 | 7 | |
| α-helix | 1872-1886 | 15 | |
| α-helix | 1893-1900 | 8 | |
| α-helix | 1908-1918 | 11 | |
| α-helix | 1923-1937 | 15 | |
| β-strand | 1947-1952 | 6 | 1 |
| α-helix | 1961-1963 | 3 | |
| β-strand | 1972-1974 | 3 | 1 |
| α-helix | 1978-1989 | 12 | |
| α-helix | 1995-1998 | 4 | |
| β-strand | 2005-2009 | 5 | 1 |
| α-helix | 2017-2027 | 11 | |
| β-strand | 2032-2036 | 5 | 1 |
| α-helix | 2039-2041 | 3 | |
| α-helix | 2042-2050 | 9 | |
| β-strand | 2054-2057 | 4 | 1 |
| α-helix | 2069-2073 | 5 | |
| β-strand | 2080-2083 | 4 | 1 |
| β-strand | 2092 | 1 | 2 |
| α-helix | 2098-2099 | 2 | |
| β-strand | 2100 | 1 | 2 |
| α-helix | 2102-2108 | 7 | |
| β-strand | 2113-2117 | 5 | 1 |
| α-helix | 2126-2138 | 13 | |
| β-strand | 2145 | 1 | 3 |
| α-helix | 2146-2152 | 7 | |
| α-helix | 2153-2155 | 3 | |
| β-strand | 2167-2171 | 5 | 1 |
| β-strand | 2175 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Separin | A | protein | 2217 | Homo sapiens | Q14674 (AlphaFold model) |
>9HMA_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 RPEQVQEALTKHDLYIYAGHGAGARFLDGQAVLRLSCRAVALLFGCSSAALAVHGNLEGA 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 9HMA 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.