Cryo-EM structure of the base of the Saccharomyces cerevisiae KMN junction complex containing the Mis12c(Mtw1c) head 2 domain. Determined by electron microscopy at 6.5 Å resolution. Released 8 Apr 2026.
Explore 9S53 in 3D Show helices and sheets RCSB PDB PDBe
9S53 contains 32 α-helices and 4 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 | 231-243 | 13 | |
| α-helix | 247-254 | 8 | |
| α-helix | 271-273 | 3 | |
| α-helix | 275-277 | 3 | |
| α-helix | 285-309 | 25 | |
| α-helix | 340-355 | 16 | |
| α-helix | 436-467 | 32 | |
| α-helix | 471-481 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| α-helix | 6-16 | 11 | |
| α-helix | 20-48 | 29 | |
| β-strand | 52 | 1 | 1 |
| β-strand | 55 | 1 | 1 |
| α-helix | 58-86 | 29 | |
| α-helix | 87-92 | 6 | |
| α-helix | 93-95 | 3 | |
| α-helix | 96-99 | 4 | |
| α-helix | 107-109 | 3 | |
| α-helix | 117-150 | 34 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-27 | 21 | |
| α-helix | 30-36 | 7 | |
| α-helix | 38-42 | 5 | |
| α-helix | 44-75 | 32 | |
| α-helix | 78-97 | 20 | |
| α-helix | 101-103 | 3 | |
| α-helix | 110-112 | 3 | |
| α-helix | 116-152 | 37 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-5 | 3 | |
| β-strand | 9-10 | 2 | 2 |
| α-helix | 13-34 | 22 | |
| α-helix | 44-65 | 22 | |
| β-strand | 68-69 | 2 | 2 |
| α-helix | 80-85 | 6 | |
| α-helix | 88-91 | 4 | |
| α-helix | 93-95 | 3 | |
| α-helix | 99-158 | 60 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinetochore-associated protein DSN1 | Ds | protein | 576 | Saccharomyces cerevisiae S288C | P40568 (AlphaFold model) |
| Kinetochore-associated protein MTW1 | Mt | protein | 289 | Saccharomyces cerevisiae S288C | P39731 (AlphaFold model) |
| Kinetochore-associated protein NNF1 | Nn | protein | 201 | Saccharomyces cerevisiae S288C | P47149 (AlphaFold model) |
| Kinetochore-associated protein NSL1 | Ns | protein | 216 | Saccharomyces cerevisiae S288C | Q12143 (AlphaFold model) |
>9S53_1 Kinetochore-associated protein DSN1 (chains Ds) MSLEPTQTVSGTPPMLHQRTHKQVYPLRMETIPILESDSKATLQSNEPTQKDEEETEYFE NKQSVSNLSPDLKFKRHKNKHIQGFPTLGERLDNLQDIKKAKRVENFNSSAPIADDNHSG DATANATANATANATANVNASAMPAPYMPYYYYYHPMNAPTPAMIPYPGSPMHSIMPNSS LQPFYSQPTAAGGPDMTTPQNISSSQQLLPAPQLFPYGSFHQQQLQQPHYIQRTRERKKS IGSQRGRRLSMLASQANGGSTIISPHKDIPEEDFYTVVGNASFGKNLQIRQLFNWCLMRS LHKLELKAKNQEEEGELEHLTKKSKLESTKAETDYVDPKRLAMVIIKEFVDDLKKDHIAI DWEDEEKYEDEDEEKILDNTENYDDTELRQLFQENDDDDDDDDEVDYSEIQRSRRKFSER RKALPKEPKKLLPNSKNVENTKNLSILTSKVNAIKNEVKEWAVTLDTSRPDLEWQELTSF SSQPLEPLSDTEEPDLAIADVETKLETKVDELRYQSHILNSHSLALNEITNSKVNKLNIE TMRKISSETDDDHSQVINPQQLLKGLSLSFSKKLDL
>9S53_2 Kinetochore-associated protein MTW1 (chains Mt) MSAPTMRSTSILTEHLGYPPISLVDDIINAVNEIMYKCTAAMEKYLLSKSKIGEEDYGEE IKSGVAKLESLLENSVDKNFDKLELYVLRNVLRIPEEYLDANVFRLENQKDLVIVDENEL KKSEEKLREKVNDVELAFKKNEMLLKRVTKVKRLLFTIRGFKQKLNELLKCKDDVQLQKI LESLKPIDDTMTLLTDSLRKLYVDSESTSSTEEVEALLQRLKTNGKQNNKDFRTRYIDIR TNNVLRKLGLLGDKEDEKQSAKPDARTQAGDIVSIDIEEPQLDLLDDVL
>9S53_3 Kinetochore-associated protein NNF1 (chains Nn) MVNSHGIRYIRLKQVFNRALDQSISKLQSWDKVSSCFPQYVNSKQGAINVANCQRQLTEF WTELCQREFKEIMEERNVEQKLNELDELILEAKERYTDRDQDEVNKGPAIDELSSKELVE CHLYSQRMHAIHEIDERLAKVNEMNDQLAQELKDLETQVEVEKNEIGKMYDEYLGSHTDQ PANVLLVQSLNDMVLELKENY
>9S53_4 Kinetochore-associated protein NSL1 (chains Ns) MSQGQSKKLDVTVEQLRSIYHQFHDILEEKTDLHLPKKEYDDDAVRREVQIQLQEFLLSA MTMASKSLEVVNADTVGKTVKQLIMESQEKYMEPFDLDLNEQVRKMYQEWEDETVKVAQL RQTGPAKINEVYNNSKDEYLAQLDGRIGVLQARMMQQQSADHDDSTDDADDHINWEHIKQ DYVASLNELYQTQQDLPKVRYNVEKVKRLMDFLEED
Assembly and phosphoregulatory mechanisms of the budding yeast outer kinetochore KMN complex. Turner, N.N., Zhang, Z., Yang, J. et al. J Cell Biol (2026) 225. DOI 10.1083/jcb.202506015 · PubMed
Other PDB entries of the same protein (UniProt P40568 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9S53 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.