9S53: Kinetochore-associated protein DSN1

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.

Method
Electron microscopy
Resolution
6.5 Å
Organism
Saccharomyces cerevisiae S288C
Chains
4
Atoms
4,985
Mol. weight
148.19 kDa
Released
8 Apr 2026

Explore 9S53 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain Ds: 8 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix231-24313
α-helix247-2548
α-helix271-2733
α-helix275-2773
α-helix285-30925
α-helix340-35516
α-helix436-46732
α-helix471-48111
Chain Mt: 9 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix2-43
α-helix6-1611
α-helix20-4829
β-strand5211
β-strand5511
α-helix58-8629
α-helix87-926
α-helix93-953
α-helix96-994
α-helix107-1093
α-helix117-15034
Chain Nn: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix7-2721
α-helix30-367
α-helix38-425
α-helix44-7532
α-helix78-9720
α-helix101-1033
α-helix110-1123
α-helix116-15237
Chain Ns: 7 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix3-53
β-strand9-1022
α-helix13-3422
α-helix44-6522
β-strand68-6922
α-helix80-856
α-helix88-914
α-helix93-953
α-helix99-15860

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Kinetochore-associated protein DSN1Dsprotein576Saccharomyces cerevisiae S288CP40568 (AlphaFold model)
Kinetochore-associated protein MTW1Mtprotein289Saccharomyces cerevisiae S288CP39731 (AlphaFold model)
Kinetochore-associated protein NNF1Nnprotein201Saccharomyces cerevisiae S288CP47149 (AlphaFold model)
Kinetochore-associated protein NSL1Nsprotein216Saccharomyces cerevisiae S288CQ12143 (AlphaFold model)
Sequence of entity 1 (Ds), FASTA
>9S53_1 Kinetochore-associated protein DSN1 (chains Ds)
MSLEPTQTVSGTPPMLHQRTHKQVYPLRMETIPILESDSKATLQSNEPTQKDEEETEYFE
NKQSVSNLSPDLKFKRHKNKHIQGFPTLGERLDNLQDIKKAKRVENFNSSAPIADDNHSG
DATANATANATANATANVNASAMPAPYMPYYYYYHPMNAPTPAMIPYPGSPMHSIMPNSS
LQPFYSQPTAAGGPDMTTPQNISSSQQLLPAPQLFPYGSFHQQQLQQPHYIQRTRERKKS
IGSQRGRRLSMLASQANGGSTIISPHKDIPEEDFYTVVGNASFGKNLQIRQLFNWCLMRS
LHKLELKAKNQEEEGELEHLTKKSKLESTKAETDYVDPKRLAMVIIKEFVDDLKKDHIAI
DWEDEEKYEDEDEEKILDNTENYDDTELRQLFQENDDDDDDDDEVDYSEIQRSRRKFSER
RKALPKEPKKLLPNSKNVENTKNLSILTSKVNAIKNEVKEWAVTLDTSRPDLEWQELTSF
SSQPLEPLSDTEEPDLAIADVETKLETKVDELRYQSHILNSHSLALNEITNSKVNKLNIE
TMRKISSETDDDHSQVINPQQLLKGLSLSFSKKLDL
Sequence of entity 2 (Mt), FASTA
>9S53_2 Kinetochore-associated protein MTW1 (chains Mt)
MSAPTMRSTSILTEHLGYPPISLVDDIINAVNEIMYKCTAAMEKYLLSKSKIGEEDYGEE
IKSGVAKLESLLENSVDKNFDKLELYVLRNVLRIPEEYLDANVFRLENQKDLVIVDENEL
KKSEEKLREKVNDVELAFKKNEMLLKRVTKVKRLLFTIRGFKQKLNELLKCKDDVQLQKI
LESLKPIDDTMTLLTDSLRKLYVDSESTSSTEEVEALLQRLKTNGKQNNKDFRTRYIDIR
TNNVLRKLGLLGDKEDEKQSAKPDARTQAGDIVSIDIEEPQLDLLDDVL
Sequence of entity 3 (Nn), FASTA
>9S53_3 Kinetochore-associated protein NNF1 (chains Nn)
MVNSHGIRYIRLKQVFNRALDQSISKLQSWDKVSSCFPQYVNSKQGAINVANCQRQLTEF
WTELCQREFKEIMEERNVEQKLNELDELILEAKERYTDRDQDEVNKGPAIDELSSKELVE
CHLYSQRMHAIHEIDERLAKVNEMNDQLAQELKDLETQVEVEKNEIGKMYDEYLGSHTDQ
PANVLLVQSLNDMVLELKENY
Sequence of entity 4 (Ns), FASTA
>9S53_4 Kinetochore-associated protein NSL1 (chains Ns)
MSQGQSKKLDVTVEQLRSIYHQFHDILEEKTDLHLPKKEYDDDAVRREVQIQLQEFLLSA
MTMASKSLEVVNADTVGKTVKQLIMESQEKYMEPFDLDLNEQVRKMYQEWEDETVKVAQL
RQTGPAKINEVYNNSKDEYLAQLDGRIGVLQARMMQQQSADHDDSTDDADDHINWEHIKQ
DYVASLNELYQTQQDLPKVRYNVEKVKRLMDFLEED

Primary citation

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:

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