Cryo-EM structure of 6-subunit Smc5/6 head region. Determined by electron microscopy at 5.58 Å resolution. Released 26 Jun 2024.
Explore 8WJN in 3D Show helices and sheets RCSB PDB PDBe
8WJN contains 84 α-helices and 48 β-strands across 5 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 |
|---|---|---|---|
| β-strand | 42-47 | 6 | 6 |
| β-strand | 57-58 | 2 | 6 |
| β-strand | 64 | 1 | 7 |
| β-strand | 66 | 1 | 8 |
| α-helix | 76-82 | 7 | |
| α-helix | 90-92 | 3 | |
| α-helix | 99-102 | 4 | |
| β-strand | 112-116 | 5 | 6 |
| α-helix | 120-122 | 3 | |
| β-strand | 135-140 | 6 | 6 |
| α-helix | 148 | 1 | |
| β-strand | 149-152 | 4 | 6 |
| β-strand | 156-157 | 2 | 6 |
| α-helix | 159-169 | 11 | |
| β-strand | 179 | 1 | 7 |
| α-helix | 182-190 | 9 | |
| α-helix | 193-204 | 12 | |
| α-helix | 207-260 | 54 | |
| α-helix | 270-273 | 4 | |
| α-helix | 274-282 | 9 | |
| α-helix | 828-832 | 5 | |
| α-helix | 834-840 | 7 | |
| α-helix | 849-856 | 8 | |
| α-helix | 863-869 | 7 | |
| α-helix | 871-874 | 4 | |
| α-helix | 875-877 | 3 | |
| α-helix | 884-947 | 64 | |
| β-strand | 950-956 | 7 | 9 |
| α-helix | 961-963 | 3 | |
| β-strand | 965-971 | 7 | 9 |
| β-strand | 979-980 | 2 | 9 |
| α-helix | 988-1002 | 15 | |
| β-strand | 1010-1013 | 4 | 7 |
| α-helix | 1023-1036 | 14 | |
| α-helix | 1041-1042 | 2 | |
| β-strand | 1043-1046 | 4 | 7 |
| β-strand | 1063 | 1 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 82-88 | 7 | 1 |
| β-strand | 90 | 1 | 2 |
| β-strand | 95-99 | 5 | 1 |
| β-strand | 106-108 | 3 | 3 |
| α-helix | 118-125 | 8 | |
| α-helix | 130-133 | 4 | |
| β-strand | 143 | 1 | 2 |
| β-strand | 149-157 | 9 | 1 |
| α-helix | 166-169 | 4 | |
| β-strand | 172-180 | 9 | 1 |
| β-strand | 188-191 | 4 | 1 |
| α-helix | 201-210 | 10 | |
| α-helix | 218-221 | 4 | |
| α-helix | 224-231 | 8 | |
| α-helix | 236-246 | 11 | |
| α-helix | 249-285 | 37 | |
| α-helix | 295-315 | 21 | |
| α-helix | 317-320 | 4 | |
| α-helix | 874-879 | 6 | |
| α-helix | 885-888 | 4 | |
| α-helix | 898-917 | 20 | |
| α-helix | 922-986 | 65 | |
| β-strand | 989-991 | 3 | 4 |
| β-strand | 994-995 | 2 | 5 |
| β-strand | 1000-1001 | 2 | 5 |
| β-strand | 1004-1006 | 3 | 4 |
| β-strand | 1014-1015 | 2 | 4 |
| α-helix | 1016-1018 | 3 | |
| α-helix | 1021-1036 | 16 | |
| β-strand | 1045-1047 | 3 | 3 |
| α-helix | 1055-1060 | 6 | |
| α-helix | 1063-1071 | 9 | |
| β-strand | 1078-1081 | 4 | 3 |
| α-helix | 1085-1088 | 4 | |
| β-strand | 1098-1100 | 3 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-27 | 14 | |
| β-strand | 31-33 | 3 | 10 |
| α-helix | 34-44 | 11 | |
| α-helix | 45-47 | 3 | |
| α-helix | 57-76 | 20 | |
| β-strand | 82-86 | 5 | 10 |
| α-helix | 91-93 | 3 | |
| α-helix | 95-97 | 3 | |
| β-strand | 131-135 | 5 | 10 |
| α-helix | 152-167 | 16 | |
| α-helix | 184-194 | 11 | |
| β-strand | 207 | 1 | 11 |
| α-helix | 213-217 | 5 | |
| α-helix | 224-236 | 13 | |
| β-strand | 241-242 | 2 | 12 |
| β-strand | 248-249 | 2 | 12 |
| α-helix | 252-258 | 7 | |
| α-helix | 260-265 | 6 | |
| β-strand | 282 | 1 | 13 |
| α-helix | 307-315 | 9 | |
| β-strand | 334 | 1 | 13 |
| β-strand | 335 | 1 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 12-24 | 13 | |
| α-helix | 26-41 | 16 | |
| β-strand | 46-47 | 2 | 14 |
| α-helix | 48-61 | 14 | |
| α-helix | 69-83 | 15 | |
| β-strand | 86-90 | 5 | 14 |
| β-strand | 122-127 | 6 | 14 |
| α-helix | 135-150 | 16 | |
| α-helix | 152-154 | 3 | |
| α-helix | 179-194 | 16 | |
| β-strand | 199-200 | 2 | 15 |
| α-helix | 201-211 | 11 | |
| α-helix | 218-220 | 3 | |
| α-helix | 227-237 | 11 | |
| β-strand | 240-247 | 8 | 15 |
| β-strand | 251-258 | 8 | 15 |
| α-helix | 260-265 | 6 | |
| α-helix | 268-279 | 12 | |
| α-helix | 284-286 | 3 | |
| α-helix | 290-297 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 44-71 | 28 | |
| α-helix | 75-90 | 16 | |
| α-helix | 100-120 | 21 | |
| α-helix | 132-139 | 8 | |
| α-helix | 200-205 | 6 | |
| α-helix | 220-226 | 7 | |
| α-helix | 242-244 | 3 | |
| α-helix | 293-300 | 8 | |
| α-helix | 308-311 | 4 | |
| α-helix | 322-325 | 4 | |
| β-strand | 330 | 1 | 16 |
| α-helix | 331-334 | 4 | |
| α-helix | 339-342 | 4 | |
| β-strand | 348 | 1 | 16 |
| α-helix | 361-363 | 3 | |
| α-helix | 364-369 | 6 | |
| α-helix | 370-372 | 3 | |
| α-helix | 388-391 | 4 |
| 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) |
| Non-structural maintenance of chromosomes element 1 | F | protein | 336 | Saccharomyces cerevisiae S288C | Q07913 (AlphaFold model) |
| Non-structural maintenance of chromosome element 3 | G | protein | 303 | Saccharomyces cerevisiae S288C | Q05541 (AlphaFold model) |
| Non-structural maintenance of chromosomes element 4 | H | protein | 402 | Saccharomyces cerevisiae S288C | A0A6L0Z6W9 |
>8WJN_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
>8WJN_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
>8WJN_3 Non-structural maintenance of chromosomes element 1 (chains F) MEVHEEQVSAPVTGDATAKYLLQYILSARGICHENALILALMRLETDASTLNTEWSIQQW VDKLNDYINAINVKLNLLGYKIIRINHGIGRNAVTLKAKQNFESFEDNTAIRAHNNDYAV LQSIVLPESNRFFVYVNLASTEETKLATRFNQNEIEFMKWAIEQFMISGETIVEGPALET SIIVKEVNRILVAATGDSNLAKWRKFSTFTVGSTNLFQFQELTATDIEDLLLRLCELKWF YRTQEGKFGIDLRCIAELEEYLTSMYNLNTCQNCHKLAIQGVRCGNESCREENEETGENS LSQIWHVDCFKHYITHVSKNCDRCGSSLITEGVYVI
>8WJN_4 Non-structural maintenance of chromosome element 3 (chains G) MSSIDNDSDVDLTEDLAVAKIVKENPVARKMVRYILSRGESQNSIITRNKLQSVIHEAAR EENIAKPSFSKMFMDINAILYNVYGFELQGLPSKNNMNAGGNGSNSNTNKSMPEPLGHRA QKFILLNNVPHSKNFDDFKILQSAHTYEELIVTGEYIGDDIASGTSNTLESKLSTDRDLV YKGVLSVILCIVFFSKNNILHQELIKFLETFGIPSDGSKIAILNITIEDLIKSLEKREYI VRLEEKSDTDGEVISYRIGRRTQAELGLESLEKLVQEIMGLEKEQTKSLHDDIIKSIGDS YSI
>8WJN_5 Non-structural maintenance of chromosomes element 4 (chains H) MSSTVISRKRRNSTVTEPDSSGETRKQKKSRSDEKSSSSKDGDPQLEFKVLQGYRDLESE MHKGRAQVTRTGDIGVAMDNLNAVDSLFNKVIGIKNNGLFAHDARAMVSISELAQISVRN LKFDDSRSMVNLENIVNSLKRYMLKEHFKLNNIAENRNDLTLAADEQSAADQQEESDGDI DRTPDDNHTDKATSSFKATSMRHSYLQQFSHYNEFSQFNWFRIGALYNTISKNAPITDHL MGPLSIEKKPRVLTQRRRNNDQVGEKITAEKITQHSLNSTQQETTPEQVKKCFKKLSKKL GPEGSINLFKFIIDPNSFSRSIENLFYTSFLIKEGKLLMEHDEEGLPTIKIKQSISHTDS RSKEIERQRRRAAHQNHIIFQMDMPTWRKLIKKYNITSPFLD
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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