Cryo-EM structure of Nse1/3/4. Determined by electron microscopy at 4.18 Å resolution. Released 31 Jan 2024.
Explore 7YMD in 3D Show helices and sheets RCSB PDB PDBe
7YMD contains 38 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 | 115-120 | 6 | |
| α-helix | 132-139 | 8 | |
| α-helix | 153-155 | 3 | |
| α-helix | 200-205 | 6 | |
| α-helix | 207-210 | 4 | |
| α-helix | 220-225 | 6 | |
| α-helix | 226-230 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 14-26 | 13 | |
| β-strand | 31-33 | 3 | 1 |
| α-helix | 34-48 | 15 | |
| α-helix | 57-76 | 20 | |
| β-strand | 81-86 | 6 | 1 |
| α-helix | 92-96 | 5 | |
| β-strand | 97 | 1 | 2 |
| β-strand | 100 | 1 | 2 |
| β-strand | 131-136 | 6 | 1 |
| α-helix | 152-167 | 16 | |
| α-helix | 182-194 | 13 | |
| β-strand | 206-207 | 2 | 3 |
| α-helix | 216-218 | 3 | |
| α-helix | 224-236 | 13 | |
| β-strand | 240-242 | 3 | 4 |
| β-strand | 248-250 | 3 | 4 |
| α-helix | 252-257 | 6 | |
| α-helix | 259-265 | 7 | |
| α-helix | 268-269 | 2 | |
| β-strand | 270 | 1 | 5 |
| β-strand | 271 | 1 | 6 |
| β-strand | 277 | 1 | 5 |
| β-strand | 281-282 | 2 | 3 |
| β-strand | 304 | 1 | 6 |
| β-strand | 305 | 1 | 3 |
| α-helix | 307-315 | 9 | |
| β-strand | 334-335 | 2 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 9-24 | 16 | |
| α-helix | 26-41 | 16 | |
| β-strand | 46-47 | 2 | 7 |
| α-helix | 48-62 | 15 | |
| α-helix | 69-79 | 11 | |
| α-helix | 80-84 | 5 | |
| β-strand | 86-91 | 6 | 7 |
| α-helix | 95-98 | 4 | |
| β-strand | 122-127 | 6 | 7 |
| α-helix | 130-131 | 2 | |
| α-helix | 135-145 | 11 | |
| α-helix | 147-150 | 4 | |
| α-helix | 152-154 | 3 | |
| α-helix | 178-194 | 17 | |
| β-strand | 199-200 | 2 | 8 |
| α-helix | 201-208 | 8 | |
| α-helix | 209-211 | 3 | |
| α-helix | 218-220 | 3 | |
| α-helix | 227-236 | 10 | |
| β-strand | 240-244 | 5 | 8 |
| β-strand | 247 | 1 | 9 |
| β-strand | 251 | 1 | 9 |
| β-strand | 254-258 | 5 | 8 |
| α-helix | 260-265 | 6 | |
| α-helix | 268-279 | 12 | |
| α-helix | 283-286 | 4 | |
| α-helix | 290-297 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Non-structural maintenance of chromosome element 4 | A | protein | 402 | Saccharomyces cerevisiae S288C | P43124 (AlphaFold model) |
| Non-structural maintenance of chromosomes element 1 | B | protein | 336 | Saccharomyces cerevisiae S288C | Q07913 (AlphaFold model) |
| Non-structural maintenance of chromosome element 3 | C | protein | 303 | Saccharomyces cerevisiae S288C | Q05541 (AlphaFold model) |
>7YMD_1 Non-structural maintenance of chromosome element 4 (chains A) MSSTVISRKRRNSTVTEPDSSGETRKQKKSRSDEKSSSSKDGDPQLEFKVLQGYRDLESE MHKGRAQVTRTGDIGVAMDNLNAVDSLFNKVIGIKNNGLFAHDARAMVSISELAQISVRN LKFDDSRSMVNLENIVNSLKRYMLKEHFKLNNIAENRNDLTLAADEQSAADQQEESDGDI DRTPDDNHTDKATSSFKATSMRHSYLQQFSHYNEFSQFNWFRIGALYNTISKNAPITDHL MGPLSIEKKPRVLTQRRRNNDQVGEKITAEKITQHSLNSTQQETTPEQVKKCFKKLSKKL GPEGSINLFKFIIDPNSFSRSIENLFYTSFLIKEGKLLMEHDEEGLPTIKIKQSISHTDS RSKEIERQRRRAAHQNHIIFQMDMPTWRKLIKKYNITSPFLD
>7YMD_2 Non-structural maintenance of chromosomes element 1 (chains B) MEVHEEQVSAPVTGDATAKYLLQYILSARGICHENALILALMRLETDASTLNTEWSIQQW VDKLNDYINAINVKLNLLGYKIIRINHGIGRNAVTLKAKQNFESFEDNTAIRAHNNDYAV LQSIVLPESNRFFVYVNLASTEETKLATRFNQNEIEFMKWAIEQFMISGETIVEGPALET SIIVKEVNRILVAATGDSNLAKWRKFSTFTVGSTNLFQFQELTATDIEDLLLRLCELKWF YRTQEGKFGIDLRCIAELEEYLTSMYNLNTCQNCHKLAIQGVRCGNESCREENEETGENS LSQIWHVDCFKHYITHVSKNCDRCGSSLITEGVYVI
>7YMD_3 Non-structural maintenance of chromosome element 3 (chains C) MSSIDNDSDVDLTEDLAVAKIVKENPVARKMVRYILSRGESQNSIITRNKLQSVIHEAAR EENIAKPSFSKMFMDINAILYNVYGFELQGLPSKNNMNAGGNGSNSNTNKSMPEPLGHRA QKFILLNNVPHSKNFDDFKILQSAHTYEELIVTGEYIGDDIASGTSNTLESKLSTDRDLV YKGVLSVILCIVFFSKNNILHQELIKFLETFGIPSDGSKIAILNITIEDLIKSLEKREYI VRLEEKSDTDGEVISYRIGRRTQAELGLESLEKLVQEIMGLEKEQTKSLHDDIIKSIGDS YSI
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 P43124 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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