Cryo-EM structure of 8-subunit Smc5/6 hinge region. Determined by electron microscopy at 6.17 Å resolution. Released 31 Jan 2024.
Explore 7YLM in 3D Show helices and sheets RCSB PDB PDBe
7YLM contains 42 α-helices and 23 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 | 349-352 | 4 | |
| α-helix | 353-356 | 4 | |
| α-helix | 357-359 | 3 | |
| α-helix | 360-363 | 4 | |
| α-helix | 365-388 | 24 | |
| α-helix | 397-446 | 50 | |
| α-helix | 453-458 | 6 | |
| α-helix | 462-474 | 13 | |
| α-helix | 486-488 | 3 | |
| β-strand | 490 | 1 | 1 |
| α-helix | 495-502 | 8 | |
| α-helix | 507-510 | 4 | |
| β-strand | 512-514 | 3 | 2 |
| α-helix | 523-525 | 3 | |
| β-strand | 535-537 | 3 | 2 |
| β-strand | 568 | 1 | 1 |
| α-helix | 570-580 | 11 | |
| α-helix | 582-584 | 3 | |
| α-helix | 594-597 | 4 | |
| α-helix | 598-600 | 3 | |
| β-strand | 613-616 | 4 | 3 |
| β-strand | 619-623 | 5 | 3 |
| β-strand | 635-639 | 5 | 3 |
| α-helix | 659-754 | 96 | |
| α-helix | 755-757 | 3 | |
| α-helix | 758-761 | 4 | |
| β-strand | 764 | 1 | 4 |
| β-strand | 766 | 1 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 390-424 | 35 | |
| α-helix | 429-486 | 58 | |
| α-helix | 489-492 | 4 | |
| α-helix | 495-497 | 3 | |
| β-strand | 509 | 1 | 5 |
| β-strand | 511 | 1 | 5 |
| α-helix | 515-518 | 4 | |
| α-helix | 538-540 | 3 | |
| α-helix | 552-557 | 6 | |
| α-helix | 558-560 | 3 | |
| β-strand | 564 | 1 | 6 |
| α-helix | 572-578 | 7 | |
| β-strand | 581 | 1 | 7 |
| β-strand | 583 | 1 | 7 |
| β-strand | 589 | 1 | 3 |
| β-strand | 590 | 1 | 6 |
| α-helix | 621-624 | 4 | |
| β-strand | 661-662 | 2 | 8 |
| β-strand | 670-671 | 2 | 8 |
| α-helix | 703-757 | 55 | |
| α-helix | 764-785 | 22 | |
| α-helix | 788-802 | 15 | |
| α-helix | 805-812 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 44-51 | 8 | |
| α-helix | 65-67 | 3 | |
| α-helix | 142-147 | 6 | |
| α-helix | 150-154 | 5 | |
| β-strand | 184 | 1 | 9 |
| β-strand | 188 | 1 | 9 |
| α-helix | 189-191 | 3 | |
| β-strand | 194-196 | 3 | 10 |
| β-strand | 203-205 | 3 | 10 |
| α-helix | 206-212 | 7 | |
| α-helix | 232-234 | 3 | |
| β-strand | 236 | 1 | 10 |
| α-helix | 242-252 | 11 | |
| α-helix | 255-264 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Structural maintenance of chromosomes protein 5 | A | protein | 1093 | Saccharomyces cerevisiae | Q08204 (AlphaFold model) |
| SMC6 isoform 1 | B | protein | 1114 | Saccharomyces cerevisiae | Q12749 (AlphaFold model) |
| MMS21 isoform 1 | C | protein | 267 | Saccharomyces cerevisiae | P38632 (AlphaFold model) |
>7YLM_1 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
>7YLM_2 SMC6 isoform 1 (chains B) MISTTISGKRPIEQVDDELLSLTAQQENEEQQQQRKRRRHQFAPMTQFNSNTLDEDSGFR SSSDVATADQDNFLEESPSGYIKKVILRNFMCHEHFELELGSRLNFIVGNNGSGKSAILT AITIGLGAKASETNRGSSLKDLIREGCYSAKIILHLDNSKYGAYQQGIFGNEIIVERIIK RDGPASFSLRSENGKEISNKKKDIQTVVDYFSVPVSNPMCFLSQDAARSFLTASTSQDKY SHFMKGTLLQEITENLLYASAIHDSAQENMALHLENLKSLKAEYEDAKKLLRELNQTSDL NERKMLLQAKSLWIDVAHNTDACKNLENEISGIQQKVDEVTEKIRNRQEKIERYTSDGTT IEAQIDAKVIYVNEKDSEHQNARELLRDVKSRFEKEKSNQAEAQSNIDQGRKKVDALNKT IAHLEEELTKEMGGDKDQMRQELEQLEKANEKLREVNNSLVVSLQDVKNEERDIQHERES ELRTISRSIQNKKVELQNIAKGNDTFLMNFDRNMDRLLRTIEQRKNEFETPAIGPLGSLV TIRKGFEKWTRSIQRAISSSLNAFVVSNPKDNRLFRDIMRSCGIRSNIPIVTYCLSQFDY SKGRAHGNYPTIVDALEFSKPEIECLFVDLSRIERIVLIEDKNEARNFLQRNPVNVNMAL SLRDRRSGFQLSGGYRLDTVTYQDKIRLKVNSSSDNGTQYLKDLIEQETKELQNIRDRYE EKLSEVRSRLKEIDGRLKSTKNEMRKTNFRMTELKMNVGKVVDTGILNSKINERKNQEQA IASYEAAKEELGLKIEQIAQEAQPIKEQYDSTKLALVEAQDELQQLKEDINSRQSKIQKY KDDTIYYEDKKKVYLENIKKIEVNVAALKEGIQRQIQNACAFCSKERIENVDLPDTQEEI KRELDKVSRMIQKAEKSLGLSQEEVIALFEKCRNKYKEGQKKYMEIDEALNRLHNSLKAR DQNYKNAEKGTCFDADMDFRASLKVRKFSGNLSFIKDTKSLEIYILTTNDEKARNVDTLS GGEKSFSQMALLLATWKPMRSRIIALDEFDVFMDQVNRKIGTTLIVKKLKDIARTQTIII TPQDIGKIADIDSSGVSIHRMRDPERQNNSNFYN
>7YLM_3 MMS21 isoform 1 (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). DOI 10.1038/s41594-024-01319-1 · PubMed
Other PDB entries of the same protein (UniProt Q08204 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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