Cryo-EM structure of 5-subunit Smc5/6 head region. Determined by electron microscopy at 6.01 Å resolution. Released 26 Jun 2024.
Explore 8I4W in 3D Show helices and sheets RCSB PDB PDBe
8I4W contains 90 α-helices and 39 β-strands across 4 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 | 29-31 | 3 | |
| α-helix | 38 | 1 | |
| β-strand | 42-50 | 9 | 1 |
| β-strand | 53-59 | 7 | 1 |
| β-strand | 65-68 | 4 | 2 |
| α-helix | 75-85 | 11 | |
| α-helix | 90-93 | 4 | |
| α-helix | 99-102 | 4 | |
| α-helix | 104 | 1 | |
| β-strand | 109-117 | 9 | 1 |
| β-strand | 134-142 | 9 | 1 |
| β-strand | 149-152 | 4 | 1 |
| β-strand | 155-158 | 4 | 1 |
| α-helix | 159-168 | 10 | |
| β-strand | 179-180 | 2 | 3 |
| α-helix | 182-189 | 8 | |
| α-helix | 193-203 | 11 | |
| α-helix | 207-253 | 47 | |
| α-helix | 891-909 | 19 | |
| α-helix | 913-944 | 32 | |
| β-strand | 953-956 | 4 | 4 |
| α-helix | 961-963 | 3 | |
| β-strand | 965-968 | 4 | 4 |
| α-helix | 977 | 1 | |
| α-helix | 988-1001 | 14 | |
| β-strand | 1012-1013 | 2 | 3 |
| α-helix | 1024-1037 | 14 | |
| β-strand | 1045 | 1 | 2 |
| β-strand | 1062-1065 | 4 | 2 |
| α-helix | 1073-1074 | 2 | |
| α-helix | 1079-1081 | 3 | |
| β-strand | 1083 | 1 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-35 | 23 | |
| α-helix | 77-78 | 2 | |
| β-strand | 82-88 | 7 | 5 |
| β-strand | 90 | 1 | 6 |
| β-strand | 96-98 | 3 | 5 |
| β-strand | 104-107 | 4 | 7 |
| α-helix | 109-110 | 2 | |
| α-helix | 117-126 | 10 | |
| α-helix | 130-133 | 4 | |
| α-helix | 139-142 | 4 | |
| β-strand | 143 | 1 | 6 |
| α-helix | 144 | 1 | |
| β-strand | 149-157 | 9 | 5 |
| α-helix | 166-169 | 4 | |
| β-strand | 172-180 | 9 | 5 |
| β-strand | 186-188 | 3 | 5 |
| β-strand | 190 | 1 | 8 |
| β-strand | 196 | 1 | 8 |
| α-helix | 202-211 | 10 | |
| β-strand | 221-222 | 2 | 7 |
| α-helix | 224-231 | 8 | |
| α-helix | 236-246 | 11 | |
| α-helix | 250-297 | 48 | |
| α-helix | 915-918 | 4 | |
| α-helix | 922-983 | 62 | |
| α-helix | 984-986 | 3 | |
| β-strand | 989-995 | 7 | 9 |
| β-strand | 1000-1006 | 7 | 9 |
| β-strand | 1014-1015 | 2 | 9 |
| α-helix | 1021-1036 | 16 | |
| β-strand | 1043-1046 | 4 | 7 |
| α-helix | 1056-1070 | 15 | |
| β-strand | 1076-1080 | 5 | 7 |
| α-helix | 1085-1087 | 3 | |
| β-strand | 1096-1099 | 4 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 143-150 | 8 | |
| α-helix | 164-172 | 9 | |
| α-helix | 182-189 | 8 | |
| β-strand | 198-199 | 2 | 10 |
| α-helix | 209-220 | 12 | |
| α-helix | 227-229 | 3 | |
| α-helix | 236-242 | 7 | |
| α-helix | 246-253 | 8 | |
| α-helix | 257-261 | 5 | |
| β-strand | 274-275 | 2 | 10 |
| β-strand | 281 | 1 | 11 |
| α-helix | 284-292 | 9 | |
| α-helix | 301-315 | 15 | |
| α-helix | 318-323 | 6 | |
| α-helix | 329-337 | 9 | |
| α-helix | 340-350 | 11 | |
| α-helix | 356-365 | 10 | |
| α-helix | 367-369 | 3 | |
| α-helix | 370-377 | 8 | |
| α-helix | 388-402 | 15 | |
| α-helix | 405-415 | 11 | |
| α-helix | 428-440 | 13 | |
| α-helix | 448-462 | 15 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12 | 1 | 12 |
| β-strand | 22 | 1 | 12 |
| α-helix | 26-40 | 15 | |
| α-helix | 44-53 | 10 | |
| α-helix | 62-65 | 4 | |
| α-helix | 66-76 | 11 | |
| α-helix | 80-90 | 11 | |
| α-helix | 100-116 | 17 | |
| α-helix | 125-141 | 17 | |
| α-helix | 143-147 | 5 | |
| α-helix | 191-193 | 3 | |
| β-strand | 197 | 1 | 13 |
| β-strand | 202 | 1 | 13 |
| α-helix | 204-208 | 5 | |
| α-helix | 214-225 | 12 | |
| α-helix | 230-234 | 5 | |
| α-helix | 235-240 | 6 | |
| α-helix | 241-257 | 17 | |
| α-helix | 258-262 | 5 | |
| α-helix | 271-277 | 7 | |
| α-helix | 280-286 | 7 | |
| α-helix | 293-301 | 9 | |
| α-helix | 308-309 | 2 | |
| α-helix | 310-312 | 3 | |
| α-helix | 313-317 | 5 | |
| β-strand | 336 | 1 | 11 |
| α-helix | 340-363 | 24 | |
| α-helix | 366 | 1 | |
| α-helix | 378-390 | 13 | |
| α-helix | 395-402 | 8 | |
| α-helix | 414-429 | 16 | |
| α-helix | 438-441 | 4 | |
| α-helix | 445-457 | 13 | |
| α-helix | 463-464 | 2 | |
| α-helix | 472-497 | 26 | |
| α-helix | 506-527 | 22 | |
| α-helix | 534-536 | 3 | |
| α-helix | 539-542 | 4 | |
| α-helix | 543-547 | 5 |
| 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) |
| DNA repair protein KRE29 | D | protein | 464 | Saccharomyces cerevisiae S288C | P40026 (AlphaFold model) |
| Non-structural maintenance of chromosome element 5 | E | protein | 556 | Saccharomyces cerevisiae S288C | Q03718 (AlphaFold model) |
>8I4W_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
>8I4W_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
>8I4W_3 DNA repair protein KRE29 (chains D) MGSVNSSPNEEFETVPDSQISGFDSPLIPTSVGSYFRDDDDDEKVHPNFISDPENDSLNS DEEFSSLENSDLNLSGAKAESGDDFDPILKRTIISKRKAPSNNEDEEIVKTPRKLVNYVP LKIFNLGDSFDDTITTTVAKLQDLKKEILDSPRSNKSIVITSNTVAKSELQKSIKFSGSI PEIYLDVVTKETISDKYKDWHFISKNCHYEQLMDLEMKDTAYSFLFGSSRSQGKVPEFVH LKCPSITNLLVLFGVNQEKCNSLKINYEKKENSRYDNLCTIFPVNKMLKFLMYFYSDDDN DDVREFFLKAFICLILDRKVFNAMESDHRLCFKVLELFNEAHFINSYFEIVDKNDFFLHY RLLQIFPHLQSALLRRRFSEKQGRTETIQQNIIKEFNEFFDCKNYKNLLYFILTMYGSKF IPFGPKCQVTEYFKDCILDISNETTNDVEISILKGILNLFSKIR
>8I4W_4 Non-structural maintenance of chromosome element 5 (chains E) MDGALINSVLYVSPRNGAHYFVELTEKHLLAFEMLNSMCLLENYDHVLLFLECQFGKSHN LAVIPFDIILVLFTLSTLSEYYKEPILRANDPYNTSRETLSRRALKLLQKYLAILKEFDS EQYNLYDLELLRCQFFLAIDTLTPKKQKWGFDRFRRTKSESGVTYRQNASVDPELDQAKT FKNPYRSYISCLEQRNTILGNRLLNLKLNEPGEFINMILWTLSNSLQESTPLFLSSHEIW MPLLEILIDLFSCRQDYFIQHEVAQNVSKSLFVQRLSESPLAVFFESLNTRNFANRFSEY VFLNCDYKLPSDNYATPVHPVYNGENTIVDTYIPTIKCSPLYKSQKSLALRRKLIGSCFK LLLRVPDGHRLITPRIVADDVIQGISRTLASFNDILQFKKFFMTENLSQESYFIPLLAEG TLSEILKDTQECVVILTLVENLSDGVSFCNEVIGLVKSKCFAFTEQCSQASYEEAVLNIE KCDVCLLVLLRYLLHLIGTEAILDAKEQLEMLHAIEKNDSGRRQWAKALNLGNDPPLLYP IVSQMFGVHDKSVIIE
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:
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