Cryo-EM structure of SA2-SCC1 complex at 2.9 angstrom. Determined by electron microscopy at 2.9 Å resolution. Released 3 Sept 2025.
Explore 9HMV in 3D Show helices and sheets RCSB PDB PDBe
9HMV contains 66 α-helices and 8 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 | 84-90 | 7 | |
| α-helix | 95-108 | 14 | |
| α-helix | 110-123 | 14 | |
| α-helix | 133-138 | 6 | |
| α-helix | 141-150 | 10 | |
| α-helix | 166-186 | 21 | |
| α-helix | 190-192 | 3 | |
| α-helix | 196-207 | 12 | |
| β-strand | 212 | 1 | 1 |
| α-helix | 213-254 | 42 | |
| α-helix | 262-288 | 27 | |
| α-helix | 289-293 | 5 | |
| α-helix | 294-296 | 3 | |
| β-strand | 299 | 1 | 2 |
| α-helix | 302-318 | 17 | |
| α-helix | 320-323 | 4 | |
| α-helix | 326-335 | 10 | |
| α-helix | 341-355 | 15 | |
| α-helix | 362-379 | 18 | |
| β-strand | 381 | 1 | 3 |
| α-helix | 384-400 | 17 | |
| α-helix | 407-414 | 8 | |
| α-helix | 415-418 | 4 | |
| β-strand | 419 | 1 | 4 |
| α-helix | 422-432 | 11 | |
| α-helix | 433-437 | 5 | |
| α-helix | 452-454 | 3 | |
| α-helix | 458-470 | 13 | |
| α-helix | 478-483 | 6 | |
| α-helix | 489-492 | 4 | |
| α-helix | 495-503 | 9 | |
| α-helix | 505-507 | 3 | |
| α-helix | 510-514 | 5 | |
| α-helix | 515-533 | 19 | |
| α-helix | 537-538 | 2 | |
| α-helix | 550-577 | 28 | |
| α-helix | 582-588 | 7 | |
| α-helix | 591-594 | 4 | |
| α-helix | 599-602 | 4 | |
| α-helix | 606-622 | 17 | |
| α-helix | 626-639 | 14 | |
| α-helix | 647-672 | 26 | |
| α-helix | 681-700 | 20 | |
| α-helix | 709-721 | 13 | |
| α-helix | 727-748 | 22 | |
| α-helix | 755-775 | 21 | |
| α-helix | 781-797 | 17 | |
| α-helix | 800-803 | 4 | |
| α-helix | 808-813 | 6 | |
| α-helix | 816-818 | 3 | |
| α-helix | 819-832 | 14 | |
| α-helix | 853-873 | 21 | |
| α-helix | 879-882 | 4 | |
| α-helix | 883-887 | 5 | |
| α-helix | 893-910 | 18 | |
| α-helix | 912-933 | 22 | |
| α-helix | 943-957 | 15 | |
| α-helix | 967-981 | 15 | |
| α-helix | 985-986 | 2 | |
| α-helix | 993-994 | 2 | |
| α-helix | 997-999 | 3 | |
| α-helix | 1000-1003 | 4 | |
| α-helix | 1004-1008 | 5 | |
| α-helix | 1012-1024 | 13 | |
| α-helix | 1038-1049 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 326 | 1 | 1 |
| β-strand | 331 | 1 | 2 |
| α-helix | 334-342 | 9 | |
| α-helix | 345-347 | 3 | |
| β-strand | 348 | 1 | 3 |
| β-strand | 353 | 1 | 4 |
| α-helix | 358-366 | 9 | |
| α-helix | 369-372 | 4 | |
| α-helix | 383-390 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cohesin subunit SA-2 | A | protein | 1271 | Homo sapiens | Q8N3U4 (AlphaFold model) |
| Double-strand-break repair protein rad21 homolog | B | protein | 241 | Homo sapiens | O60216 (AlphaFold model) |
>9HMV_1 Cohesin subunit SA-2 (chains A) MIAAPEIPTDFNLLQESETHFSSDTDFEDIEGKNQKQGKGKTCKKGKKGPAEKGKGGNGG GKPPSGPNRMNGHHQQNGVENMMLFEVVKMGKSAMQSVVDDWIESYKHDRDIALLDLINF FIQCSGCKGVVTAEMFRHMQNSEIIRKMTEEFDEDSGDYPLTMAGPQWKKFKSSFCEFIG VLVRQCQYSIIYDEYMMDTVISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSIN MDNTQRQYEAERNKMIGKRANERLELLLQKRKELQENQDEIENMMNAIFKGVFVHRYRDA IAEIRAICIEEIGIWMKMYSDAFLNDSYLKYVGWTMHDKQGEVRLKCLTALQGLYYNKEL NSKLELFTSRFKDRIVSMTLDKEYDVAVQAIKLLTLVLQSSEEVLTAEDCENVYHLVYSA HRPVAVAAGEFLYKKLFSRRDPEEDGMMKRRGRQGPNANLVKTLVFFFLESELHEHAAYL VDSMWDCATELLKDWECMNSLLLEEPLSGEEALTDRQESALIEIMLCTIRQAAECHPPVG RGTGKRVLTAKEKKTQLDDRTKITELFAVALPQLLAKYSVDAEKVTNLLQLPQYFDLEIY TTGRLEKHLDALLRQIRNIVEKHTDTDVLEACSKTYHALCNEEFTIFNRVDISRSQLIDE LADKFNRLLEDFLQEGEEPDEDDAYQVLSTLKRITAFHNAHDLSKWDLFACNYKLLKTGI ENGDMPEQIVIHALQCTHYVILWQLAKITESSSTKEDLLRLKKQMRVFCQICQHYLTNVN TTVKEQAFTILCDILMIFSHQIMSGGRDMLEPLVYTPDSSLQSELLSFILDHVFIEQDDD NNSADGQQEDEASKIEALHKRRNLLAAFCKLIVYTVVEMNTAADIFKQYMKYYNDYGDII KETMSKTRQIDKIQCAKTLILSLQQLFNEMIQENGYNFDRSSSTFSGIKELARRFALTFG LDQLKTREAIAMLHKDGIEFAFKEPNPQGESHPPLNLAFLDILSEFSSKLLRQDKRTVYV YLEKFMTFQMSLRREDVWLPLMSYRNSLLAGGDDDTMSVISGISSRGSTVRSKKSKPSTG KRKVVEGMQLSLTEESSSSDSMWLSREQTLHTPVMMQTPQLTSTIMREPKRLRPEDSFMS VYPMQTEHHQTPLDYNRRGTSLMEDDEEPIVEDVMMSSEGRIEDLNEGMDFDTMDIDLPP SKNRRERTELKPDFFDPASIMDESVLGVSMFSSLAEENLYFQSWSHPQFEKGGGSGGGSG GGSWSHPQFEK
>9HMV_2 Double-strand-break repair protein rad21 homolog (chains B) DITVKETKAKRKRKLIVDSVKELDSKTIRAQLSDYSDIVTTLDLAPPTKKLMMWKETGGV EKLFSLPAQPLWNNRLLKLFTRCLTPLVPEDLRKRRKGGEADNLDEFLKEFENPEVPRED QQQQHQQRDVIDEPIIEEPSRLQESVMEASRTNIDESAMPPPPPQGVKRKAGQIDPEPVM PPQQVEQMEIPPVELPPEEPPNICQLIPELELLPEKEKEKEKEKEDDEEEEDEDASGGDQ D
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 Q8N3U4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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