Cryo-EM structure of 5-subunit Smc5/6 hinge region. Determined by electron microscopy at 6.73 Å resolution. Released 26 Jun 2024.
Explore 8I4U in 3D Show helices and sheets RCSB PDB PDBe
8I4U contains 49 α-helices and 27 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 | 332-334 | 3 | |
| α-helix | 336-385 | 50 | |
| α-helix | 386-388 | 3 | |
| α-helix | 396-444 | 49 | |
| α-helix | 452-458 | 7 | |
| α-helix | 460-473 | 14 | |
| α-helix | 476-479 | 4 | |
| β-strand | 482-483 | 2 | 1 |
| α-helix | 486-489 | 4 | |
| β-strand | 491 | 1 | 2 |
| α-helix | 495-498 | 4 | |
| α-helix | 499-501 | 3 | |
| α-helix | 507-510 | 4 | |
| β-strand | 512 | 1 | 3 |
| β-strand | 514-515 | 2 | 1 |
| α-helix | 520-524 | 5 | |
| α-helix | 526-530 | 5 | |
| β-strand | 535 | 1 | 3 |
| α-helix | 551-553 | 3 | |
| β-strand | 560-561 | 2 | 4 |
| α-helix | 562-565 | 4 | |
| β-strand | 567 | 1 | 2 |
| α-helix | 570-579 | 10 | |
| β-strand | 586-587 | 2 | 4 |
| α-helix | 595-600 | 6 | |
| α-helix | 610-612 | 3 | |
| β-strand | 613 | 1 | 5 |
| β-strand | 616 | 1 | 5 |
| β-strand | 619-623 | 5 | 5 |
| β-strand | 635-639 | 5 | 5 |
| α-helix | 640-641 | 2 | |
| α-helix | 654-656 | 3 | |
| α-helix | 657-662 | 6 | |
| α-helix | 663-736 | 74 | |
| α-helix | 741-743 | 3 | |
| α-helix | 744-767 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 371-376 | 6 | |
| α-helix | 377-415 | 39 | |
| α-helix | 420-425 | 6 | |
| α-helix | 430-432 | 3 | |
| α-helix | 436-479 | 44 | |
| α-helix | 482-497 | 16 | |
| α-helix | 506-508 | 3 | |
| α-helix | 514-524 | 11 | |
| β-strand | 540-542 | 3 | 6 |
| α-helix | 543 | 1 | |
| α-helix | 553-556 | 4 | |
| α-helix | 569-573 | 5 | |
| β-strand | 616-618 | 3 | 6 |
| α-helix | 621-624 | 4 | |
| α-helix | 625-629 | 5 | |
| β-strand | 636-641 | 6 | 7 |
| α-helix | 649-651 | 3 | |
| β-strand | 658-662 | 5 | 7 |
| β-strand | 668-672 | 5 | 7 |
| β-strand | 676-679 | 4 | 7 |
| α-helix | 694-697 | 4 | |
| α-helix | 698-708 | 11 | |
| α-helix | 711-757 | 47 | |
| α-helix | 765-768 | 4 | |
| α-helix | 771-814 | 44 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 33-48 | 16 | |
| α-helix | 60-81 | 22 | |
| α-helix | 142-144 | 3 | |
| α-helix | 145-148 | 4 | |
| α-helix | 150-155 | 6 | |
| β-strand | 169 | 1 | 8 |
| β-strand | 172 | 1 | 8 |
| β-strand | 183 | 1 | 9 |
| β-strand | 190 | 1 | 9 |
| β-strand | 195-196 | 2 | 10 |
| β-strand | 203-204 | 2 | 10 |
| β-strand | 217 | 1 | 11 |
| β-strand | 219 | 1 | 11 |
| β-strand | 236 | 1 | 10 |
| α-helix | 240-262 | 23 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Structural maintenance of chromosomes protein 5 | A | protein | 1093 | Saccharomyces cerevisiae S288C | Q08204 (AlphaFold model) |
| Structural maintenance of chromosomes protein 6 | B | protein | 1114 | Saccharomyces cerevisiae S288C | Q12749 (AlphaFold model) |
| E3 SUMO-protein ligase MMS21 | C | protein | 267 | Saccharomyces cerevisiae S288C | P38632 (AlphaFold model) |
>8I4U_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
>8I4U_2 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
>8I4U_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 Q08204 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8I4U 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.