Structure of the SA2/SCC1/MCM3 complex. Determined by X-ray diffraction at 3.07 Å resolution. Released 22 Jul 2026.
Explore 9HX9 in 3D Show helices and sheets RCSB PDB PDBe
9HX9 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 | 83-89 | 7 | |
| α-helix | 95-108 | 14 | |
| α-helix | 110-124 | 15 | |
| α-helix | 133-138 | 6 | |
| α-helix | 141-150 | 10 | |
| α-helix | 160-162 | 3 | |
| α-helix | 166-185 | 20 | |
| α-helix | 190-192 | 3 | |
| α-helix | 196-207 | 12 | |
| β-strand | 212 | 1 | 1 |
| α-helix | 213-254 | 42 | |
| α-helix | 261-288 | 28 | |
| 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 | 359-361 | 3 | |
| α-helix | 365-376 | 12 | |
| α-helix | 377-380 | 4 | |
| β-strand | 381 | 1 | 3 |
| α-helix | 384-399 | 16 | |
| α-helix | 407-414 | 8 | |
| α-helix | 415-418 | 4 | |
| β-strand | 419 | 1 | 4 |
| α-helix | 422-436 | 15 | |
| α-helix | 458-470 | 13 | |
| α-helix | 478-484 | 7 | |
| α-helix | 489-492 | 4 | |
| α-helix | 495-503 | 9 | |
| α-helix | 515-533 | 19 | |
| α-helix | 537-538 | 2 | |
| α-helix | 550-578 | 29 | |
| α-helix | 582-588 | 7 | |
| α-helix | 591-593 | 3 | |
| α-helix | 598-602 | 5 | |
| α-helix | 606-622 | 17 | |
| α-helix | 626-639 | 14 | |
| α-helix | 647-672 | 26 | |
| α-helix | 681-700 | 20 | |
| α-helix | 704-706 | 3 | |
| α-helix | 709-722 | 14 | |
| 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 | 819-832 | 14 | |
| α-helix | 850-873 | 24 | |
| α-helix | 879-882 | 4 | |
| α-helix | 883-886 | 4 | |
| α-helix | 893-910 | 18 | |
| α-helix | 912-934 | 23 | |
| α-helix | 943-957 | 15 | |
| α-helix | 967-981 | 15 | |
| α-helix | 989-991 | 3 | |
| α-helix | 997-999 | 3 | |
| α-helix | 1000-1003 | 4 | |
| α-helix | 1004-1009 | 6 | |
| α-helix | 1012-1023 | 12 | |
| α-helix | 1030-1032 | 3 | |
| α-helix | 1039-1047 | 9 |
| 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 | 354-355 | 2 | |
| α-helix | 358-366 | 9 | |
| α-helix | 369-374 | 6 | |
| α-helix | 383-390 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cohesin subunit SA-2 | A | protein | 981 | Homo sapiens | Q8N3U4 (AlphaFold model) |
| 64-kDa C-terminal product | B | protein | 140 | Homo sapiens | O60216 (AlphaFold model) |
| DNA replication licensing factor MCM3 | C | protein | 12 | Homo sapiens | P25205 (AlphaFold model) |
>9HX9_1 Cohesin subunit SA-2 (chains A) ENMMLFEVVKMGKSAMQSVVDDWIESYKHDRDIALLDLINFFIQCSGCKGVVTAEMFRHM QNSEIIRKMTEEFDEDSGDYPLTMAGPQWKKFKSSFCEFIGVLVRQCQYSIIYDEYMMDT VISLLTGLSDSQVRAFRHTSTLAAMKLMTALVNVALNLSINMDNTQRQYEAERNKMIGKR ANERLELLLQKRKELQENQDEIENMMNAIFKGVFVHRYRDAIAEIRAICIEEIGIWMKMY SDAFLNDSYLKYVGWTMHDKQGEVRLKCLTALQGLYYNKELNSKLELFTSRFKDRIVSMT LDKEYDVAVQAIKLLTLVLQSSEEVLTAEDCENVYHLVYSAHRPVAVAAGEFLYKKLFSR RDPEEDGMMKRRGRQGPNANLVKTLVFFFLESELHEHAAYLVDSMWDCATELLKDWECMN SLLLEEPLSGEEALTDRQESALIEIMLCTIRQAAECHPPVGRGTGKRVLTAKEKKTQLDD RTKITELFAVALPQLLAKYSVDAEKVTNLLQLPQYFDLEIYTTGRLEKHLDALLRQIRNI VEKHTDTDVLEACSKTYHALCNEEFTIFNRVDISRSQLIDELADKFNRLLEDFLQEGEEP DEDDAYQVLSTLKRITAFHNAHDLSKWDLFACNYKLLKTGIENGDMPEQIVIHALQCTHY VILWQLAKITESSSTKEDLLRLKKQMRVFCQICQHYLTNVNTTVKEQAFTILCDILMIFS HQIMSGGRDMLEPLVYTPDSSLQSELLSFILDHVFIEQDDDNNSADGQQEDEASKIEALH KRRNLLAAFCKLIVYTVVEMNTAADIFKQYMKYYNDYGDIIKETMSKTRQIDKIQCAKTL ILSLQQLFNEMIQENGYNFDRSSSTFSGIKELARRFALTFGLDQLKTREAIAMLHKDGIE FAFKEPNPQGESHPPLNLAFLDILSEFSSKLLRQDKRTVYVYLEKFMTFQMSLRREDVWL PLMSYRNSLLAGGDDDTMSVI
>9HX9_2 64-kDa C-terminal product (chains B) VDPVEPMPTMTDQTTLVPNEEEAFALEPIDITVKETKAKRKRKLIVDSVKELDSKTIRAQ LSDYSDIVTTLDLAPPTKKLMMWKETGGVEKLFSLPAQPLWNNRLLKLFTRCLTPLVPED LRKRRKGGEADNLDEFLKEF
>9HX9_3 DNA replication licensing factor MCM3 (chains C) SYDPYDFSDTEE
A shared principle by which CTCF and MCM3 control sister chromatid cohesion. Patel, A., Panne, D. To be published.
Other PDB entries of the same protein (UniProt Q8N3U4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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