cryoEM structure of Smc5/6 5mer. Determined by electron microscopy at 3.3 Å resolution. Released 15 Nov 2023.
Explore 8T8E in 3D Show helices and sheets RCSB PDB PDBe
8T8E contains 60 α-helices and 24 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 | 77-78 | 2 | |
| β-strand | 82-88 | 7 | 1 |
| β-strand | 97-99 | 3 | 1 |
| β-strand | 104 | 1 | 2 |
| β-strand | 107 | 1 | 3 |
| α-helix | 115-124 | 10 | |
| α-helix | 144 | 1 | |
| β-strand | 150-157 | 8 | 1 |
| α-helix | 166-169 | 4 | |
| β-strand | 172-179 | 8 | 1 |
| α-helix | 184-185 | 2 | |
| β-strand | 186 | 1 | 1 |
| β-strand | 189-190 | 2 | 1 |
| β-strand | 196-198 | 3 | 1 |
| α-helix | 201-210 | 10 | |
| β-strand | 221 | 1 | 4 |
| α-helix | 224-230 | 7 | |
| α-helix | 236-246 | 11 | |
| α-helix | 252-255 | 4 | |
| α-helix | 259-262 | 4 | |
| α-helix | 952-958 | 7 | |
| α-helix | 961-965 | 5 | |
| α-helix | 974-980 | 7 | |
| β-strand | 989-995 | 7 | 5 |
| β-strand | 1000-1006 | 7 | 5 |
| β-strand | 1014-1015 | 2 | 5 |
| α-helix | 1021-1036 | 16 | |
| β-strand | 1043-1044 | 2 | 6 |
| β-strand | 1045 | 1 | 4 |
| β-strand | 1047 | 1 | 3 |
| α-helix | 1055-1070 | 16 | |
| β-strand | 1076-1077 | 2 | 6 |
| β-strand | 1080 | 1 | 3 |
| β-strand | 1096 | 1 | 2 |
| β-strand | 1099 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 209-219 | 11 | |
| α-helix | 246-253 | 8 | |
| α-helix | 271-273 | 3 | |
| β-strand | 281 | 1 | 8 |
| α-helix | 284-291 | 8 | |
| α-helix | 292-294 | 3 | |
| α-helix | 301-315 | 15 | |
| α-helix | 318-321 | 4 | |
| α-helix | 330-336 | 7 | |
| α-helix | 340-345 | 6 | |
| α-helix | 357-362 | 6 | |
| α-helix | 367-369 | 3 | |
| α-helix | 370-377 | 8 | |
| α-helix | 388-397 | 10 | |
| α-helix | 409-415 | 7 | |
| α-helix | 433-439 | 7 | |
| α-helix | 453-459 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 23-25 | 3 | |
| α-helix | 26-40 | 15 | |
| α-helix | 44-52 | 9 | |
| α-helix | 63-65 | 3 | |
| α-helix | 72-75 | 4 | |
| α-helix | 85-90 | 6 | |
| α-helix | 100-108 | 9 | |
| α-helix | 112-115 | 4 | |
| α-helix | 125-139 | 15 | |
| β-strand | 198 | 1 | 7 |
| β-strand | 201 | 1 | 7 |
| α-helix | 205-208 | 4 | |
| α-helix | 216-223 | 8 | |
| α-helix | 230-233 | 4 | |
| α-helix | 234-236 | 3 | |
| α-helix | 241-258 | 18 | |
| α-helix | 269-272 | 4 | |
| α-helix | 273-275 | 3 | |
| α-helix | 280-286 | 7 | |
| α-helix | 297-300 | 4 | |
| α-helix | 314-317 | 4 | |
| β-strand | 336 | 1 | 8 |
| α-helix | 340-346 | 7 | |
| α-helix | 348-355 | 8 | |
| α-helix | 389-391 | 3 | |
| α-helix | 395-402 | 8 | |
| α-helix | 414-429 | 16 | |
| α-helix | 439-441 | 3 | |
| α-helix | 445-457 | 13 | |
| α-helix | 472-496 | 25 | |
| α-helix | 506-527 | 22 | |
| α-helix | 539-546 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Structural maintenance of chromosomes protein 6 | A | protein | 1114 | Saccharomyces cerevisiae W303 | Q12749 (AlphaFold model) |
| Non-structural maintenance of chromosome element 5 | C | protein | 556 | Saccharomyces cerevisiae W303 | Q03718 (AlphaFold model) |
| DNA repair protein KRE29 | B | protein | 464 | Saccharomyces cerevisiae W303 | P40026 (AlphaFold model) |
>8T8E_1 Structural maintenance of chromosomes protein 6 (chains A) MISTTISGKRPIEQVDDELLSLTAQQENEEQQQQRKRRRHQFAPMTQFNSNTLDEDSGFR SSSDVATADQDNFLEESPSGYIKKVILRNFMCHEHFELELGSRLNFIVGNNGSGKSAILT AITIGLGAKASETNRGSSLKDLIREGCYSAKIILHLDNSKYGAYQQGIFGNEIIVERIIK RDGPASFSLRSENGKEISNKKKDIQTVVDYFSVPVSNPMCFLSQDAARSFLTASTSQDKY SHFMKGTLLQEITENLLYASAIHDSAQENMALHLENLKSLKAEYEDAKKLLRELNQTSDL NERKMLLQAKSLWIDVAHNTDACKNLENEISGIQQKVDEVTEKIRNRQEKIERYTSDGTT IEAQIDAKVIYVNEKDSEHQNARELLRDVKSRFEKEKSNQAEAQSNIDQGRKKVDALNKT IAHLEEELTKEMGGDKDQMRQELEQLEKANEKLREVNNSLVVSLQDVKNEERDIQHERES ELRTISRSIQNKKVELQNIAKGNDTFLMNFDRNMDRLLRTIEQRKNEFETPAIGPLGSLV TIRKGFEKWTRSIQRAISSSLNAFVVSNPKDNRLFRDIMRSCGIRSNIPIVTYCLSQFDY SKGRAHGNYPTIVDALEFSKPEIECLFVDLSRIERIVLIEDKNEARNFLQRNPVNVNMAL SLRDRRSGFQLSGGYRLDTVTYQDKIRLKVNSSSDNGTQYLKDLIEQETKELQNIRDRYE EKLSEVRSRLKEIDGRLKSTKNEMRKTNFRMTELKMNVGKVVDTGILNSKINERKNQEQA IASYEAAKEELGLKIEQIAQEAQPIKEQYDSTKLALVEAQDELQQLKEDINSRQSKIQKY KDDTIYYEDKKKVYLENIKKIEVNVAALKEGIQRQIQNACAFCSKERIENVDLPDTQEEI KRELDKVSRMIQKAEKSLGLSQEEVIALFEKCRNKYKEGQKKYMEIDEALNRLHNSLKAR DQNYKNAEKGTCFDADMDFRASLKVRKFSGNLSFIKDTKSLEIYILTTNDEKARNVDTLS GGEKSFSQMALLLATWKPMRSRIIALDQFDVFMDQVNRKIGTTLIVKKLKDIARTQTIII TPQDIGKIADIDSSGVSIHRMRDPERQNNSNFYN
>8T8E_2 Non-structural maintenance of chromosome element 5 (chains C) MDGALINSVLYVSPRNGAHYFVELTEKHLLAFEMLNSMCLLENYDHVLLFLECQFGKSHN LAVIPFDIILVLFTLSTLSEYYKEPILRANDPYNTSRETLSRRALKLLQKYLAILKEFDS EQYNLYDLELLRCQFFLAIDTLTPKKQKWGFDRFRRTKSESGVTYRQNASVDPELDQAKT FKNPYRSYISCLEQRNTILGNRLLNLKLNEPGEFINMILWTLSNSLQESTPLFLSSHEIW MPLLEILIDLFSCRQDYFIQHEVAQNVSKSLFVQRLSESPLAVFFESLNTRNFANRFSEY VFLNCDYKLPSDNYATPVHPVYNGENTIVDTYIPTIKCSPLYKSQKSLALRRKLIGSCFK LLLRVPDGHRLITPRIVADDVIQGISRTLASFNDILQFKKFFMTENLSQESYFIPLLAEG TLSEILKDTQECVVILTLVENLSDGVSFCNEVIGLVKSKCFAFTEQCSQASYEEAVLNIE KCDVCLLVLLRYLLHLIGTEAILDAKEQLEMLHAIEKNDSGRRQWAKALNLGNDPPLLYP IVSQMFGVHDKSVIIE
>8T8E_3 DNA repair protein KRE29 (chains B) MGSVNSSPNEEFETVPDSQISGFDSPLIPTSVGSYFRDDDDDEKVHPNFISDPENDSLNS DEEFSSLENSDLNLSGAKAESGDDFDPILKRTIISKRKAPSNNEDEEIVKTPRKLVNYVP LKIFNLGDSFDDTITTTVAKLQDLKKEILDSPRSNKSIVITSNTVAKSELQKSIKFSGSI PEIYLDVVTKETISDKYKDWHFISKNCHYEQLMDLEMKDTAYSFLFGSSRSQGKVPEFVH LKCPSITNLLVLFGVNQEKCNSLKINYEKKENSRYDNLCTIFPVNKMLKFLMYFYSDDDN DDVREFFLKAFICLILDRKVFNAMESDHRLCFKVLELFNEAHFINSYFEIVDKNDFFLHY RLLQIFPHLQSALLRRRFSEKQGRTETIQQNIIKEFNEFFDCKNYKNLLYFILTMYGSKF IPFGPKCQVTEYFKDCILDISNETTNDVEISILKGILNLFSKIR
Molecular basis for Nse5-6 mediated regulation of Smc5/6 functions. Li, S., Yu, Y., Zheng, J. et al. Proc Natl Acad Sci U S A (2023) 120:e2310924120-e2310924120. DOI 10.1073/pnas.2310924120 · 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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