Cryo-EM structure of 6-subunit Smc5/6 hinge region. Determined by electron microscopy at 6.15 Å resolution. Released 26 Jun 2024.
Explore 8WJL in 3D Show helices and sheets RCSB PDB PDBe
8WJL contains 48 α-helices and 25 β-strands across 3 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 | 333-345 | 13 | |
| α-helix | 348-384 | 37 | |
| α-helix | 397-441 | 45 | |
| α-helix | 445-447 | 3 | |
| α-helix | 453-458 | 6 | |
| α-helix | 460-462 | 3 | |
| α-helix | 463-472 | 10 | |
| α-helix | 478-481 | 4 | |
| β-strand | 482-483 | 2 | 5 |
| α-helix | 485 | 1 | |
| α-helix | 486-489 | 4 | |
| β-strand | 492 | 1 | 6 |
| α-helix | 495-504 | 10 | |
| α-helix | 507-510 | 4 | |
| β-strand | 514-515 | 2 | 5 |
| α-helix | 520-523 | 4 | |
| α-helix | 547-549 | 3 | |
| β-strand | 560-561 | 2 | 7 |
| α-helix | 562-565 | 4 | |
| β-strand | 566 | 1 | 6 |
| α-helix | 575-577 | 3 | |
| α-helix | 582-584 | 3 | |
| β-strand | 586-587 | 2 | 7 |
| β-strand | 603-604 | 2 | 8 |
| β-strand | 608-609 | 2 | 8 |
| β-strand | 613-614 | 2 | 9 |
| β-strand | 621-622 | 2 | 9 |
| β-strand | 636 | 1 | 3 |
| α-helix | 660-662 | 3 | |
| α-helix | 663-707 | 45 | |
| α-helix | 710-765 | 56 | |
| α-helix | 768-773 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 370-376 | 7 | |
| α-helix | 377-430 | 54 | |
| α-helix | 435-461 | 27 | |
| α-helix | 466-490 | 25 | |
| α-helix | 491-493 | 3 | |
| α-helix | 515-521 | 7 | |
| α-helix | 525-527 | 3 | |
| β-strand | 541-542 | 2 | 1 |
| α-helix | 547-552 | 6 | |
| α-helix | 554-557 | 4 | |
| α-helix | 558-562 | 5 | |
| β-strand | 566 | 1 | 2 |
| α-helix | 569-578 | 10 | |
| α-helix | 579-582 | 4 | |
| β-strand | 591 | 1 | 3 |
| β-strand | 592 | 1 | 2 |
| β-strand | 611 | 1 | 4 |
| α-helix | 612-615 | 4 | |
| β-strand | 616-617 | 2 | 1 |
| α-helix | 622-630 | 9 | |
| α-helix | 633-635 | 3 | |
| β-strand | 637-638 | 2 | 4 |
| α-helix | 647-650 | 4 | |
| β-strand | 659-664 | 6 | 4 |
| β-strand | 667-673 | 7 | 4 |
| β-strand | 676-680 | 5 | 4 |
| β-strand | 690 | 1 | 1 |
| α-helix | 697-700 | 4 | |
| α-helix | 703-760 | 58 | |
| α-helix | 770-816 | 47 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 33-35 | 3 | |
| α-helix | 36-51 | 16 | |
| α-helix | 60-80 | 21 | |
| α-helix | 138-140 | 3 | |
| α-helix | 144-146 | 3 | |
| β-strand | 194-196 | 3 | 10 |
| β-strand | 204-205 | 2 | 10 |
| α-helix | 232-234 | 3 | |
| α-helix | 235 | 1 | |
| β-strand | 236-237 | 2 | 10 |
| α-helix | 242-266 | 25 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Structural maintenance of chromosomes protein 6 | B | protein | 1114 | Saccharomyces cerevisiae S288C | Q12749 (AlphaFold model) |
| Structural maintenance of chromosomes protein 5 | A | protein | 1093 | Saccharomyces cerevisiae S288C | Q08204 (AlphaFold model) |
| E3 SUMO-protein ligase MMS21 | C | protein | 267 | Saccharomyces cerevisiae S288C | P38632 (AlphaFold model) |
>8WJL_1 Structural maintenance of chromosomes protein 6 (chains B) MISTTISGKRPIEQVDDELLSLTAQQENEEQQQQRKRRRHQFAPMTQFNSNTLDEDSGFR SSSDVATADQDNFLEESPSGYIKKVILRNFMCHEHFELELGSRLNFIVGNNGSGKSAILT AITIGLGAKASETNRGSSLKDLIREGCYSAKIILHLDNSKYGAYQQGIFGNEIIVERIIK RDGPASFSLRSENGKEISNKKKDIQTVVDYFSVPVSNPMCFLSQDAARSFLTASTSQDKY SHFMKGTLLQEITENLLYASAIHDSAQENMALHLENLKSLKAEYEDAKKLLRELNQTSDL NERKMLLQAKSLWIDVAHNTDACKNLENEISGIQQKVDEVTEKIRNRQEKIERYTSDGTT IEAQIDAKVIYVNEKDSEHQNARELLRDVKSRFEKEKSNQAEAQSNIDQGRKKVDALNKT IAHLEEELTKEMGGDKDQMRQELEQLEKANEKLREVNNSLVVSLQDVKNEERDIQHERES ELRTISRSIQNKKVELQNIAKGNDTFLMNFDRNMDRLLRTIEQRKNEFETPAIGPLGSLV TIRKGFEKWTRSIQRAISSSLNAFVVSNPKDNRLFRDIMRSCGIRSNIPIVTYCLSQFDY SKGRAHGNYPTIVDALEFSKPEIECLFVDLSRIERIVLIEDKNEARNFLQRNPVNVNMAL SLRDRRSGFQLSGGYRLDTVTYQDKIRLKVNSSSDNGTQYLKDLIEQETKELQNIRDRYE EKLSEVRSRLKEIDGRLKSTKNEMRKTNFRMTELKMNVGKVVDTGILNSKINERKNQEQA IASYEAAKEELGLKIEQIAQEAQPIKEQYDSTKLALVEAQDELQQLKEDINSRQSKIQKY KDDTIYYEDKKKVYLENIKKIEVNVAALKEGIQRQIQNACAFCSKERIENVDLPDTQEEI KRELDKVSRMIQKAEKSLGLSQEEVIALFEKCRNKYKEGQKKYMEIDEALNRLHNSLKAR DQNYKNAEKGTCFDADMDFRASLKVRKFSGNLSFIKDTKSLEIYILTTNDEKARNVDTLS GGEKSFSQMALLLATWKPMRSRIIALDEFDVFMDQVNRKIGTTLIVKKLKDIARTQTIII TPQDIGKIADIDSSGVSIHRMRDPERQNNSNFYN
>8WJL_2 Structural maintenance of chromosomes protein 5 (chains A) MTSLIDLGRYVERTHHGEDTEPRSKRVKIAKPDLSSFQPGSIIKIRLQDFVTYTLTEFNL SPSLNMIIGPNGSGKSTFVCAVCLGLAGKPEYIGRSKKVEDFIKNGQDVSKIEITLKNSP NVTDIEYIDARDETIKITRIITRSKRRSDYLINDYQVSESVVKTLVAQLNIQLDNLCQFL SQERVEEFARLKSVKLLVETIRSIDASLLDVLDELRELQGNEQSLQKDLDFKKAKIVHLR QESDKLRKSVESLRDFQNKKGEIELHSQLLPYVKVKDHKEKLNIYKEEYERAKANLRAIL KDKKPFANTKKTLENQVEELTEKCSLKTDEFLKAKEKINEIFEKLNTIRDEVIKKKNQNE YYRGRTKKLQATIISTKEDFLRSQEILAQTHLPEKSVFEDIDIKRKEIINKEGEIRDLIS EIDAKANAINHEMRSIQRQAESKTKSLTTTDKIGILNQDQDLKEVRDAVLMVREHPEMKD KILEPPIMTVSAINAQFAAYLAQCVDYNTSKALTVVDSDSYKLFANPILDKFKVNLRELS SADTTPPVPAETVRDLGFEGYLSDFITGDKRVMKMLCQTSKIHTIPVSRRELTPAQIKKL ITPRPNGKILFKRIIHGNRLVDIKQSAYGSKQVFPTDVSIKQTNFYQGSIMSNEQKIRIE NEIINLKNEYNDRKSTLDALSNQKSGYRHELSELASKNDDINREAHQLNEIRKKYTMRKS TIETLREKLDQLKREARKDVSQKIKDIDDQIQQLLLKQRHLLSKMASSMKSLKNCQKELI STQILQFEAQNMDVSMNDVIGFFNEREADLKSQYEDKKKFVKEMRDTPEFQSWMREIRSY DQDTKEKLNKVAEKYEEEGNFNLSFVQDVLDKLESEIAMVNHDESAVTILDQVTAELREL EHTVPQQSKDLETIKAKLKEDHAVLEPKLDDIVSKISARFARLFNNVGSAGAVRLEKPKD YAEWKIEIMVKFRDNAPLKKLDSHTQSGGERAVSTVLYMIALQEFTSAPFRVVDEINQGM DSRNERIVHKAMVENACAENTSQYFLITPKLLTGLHYHEKMRIHCVMAGSWIPNPSEDPK MIHFGETSNYSFD
>8WJL_3 E3 SUMO-protein ligase MMS21 (chains C) MALNDNPIPKSVPLHPKSGKYFHNLHARDLSNIYQQCYKQIDETINQLVDSTSPSTIGIE EQVADITSTYKLLSTYESESNSFDEHIKDLKKNFKQSSDACPQIDLSTWDKYRTGELTAP KLSELYLNMPTPEPATMVNNTDTLKILKVLPYIWNDPTCVIPDLQNPADEDDLQIEGGKI ELTCPITCKPYEAPLISRKCNHVFDRDGIQNYLQGYTTRDCPQAACSQVVSMRDFVRDPI MELRCKIAKMKESQEQDKRSSQAIDVL
Cryo-EM structures of Smc5/6 in multiple states reveal its assembly and functional mechanisms. Li, Q., Zhang, J., Haluska, C. et al. Nat Struct Mol Biol (2024) 31:1532-1542. DOI 10.1038/s41594-024-01319-1 · PubMed
Other PDB entries of the same protein (UniProt Q12749 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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