9S4Q: Kinetochore-associated protein NNF1
Cryo-EM structure of the Saccharomyces cerevisiae KMN junction complex lacking the Mis12c(Mtw1c) head 2 domain. Determined by electron microscopy at 4.9 Å resolution. Released 8 Apr 2026.
- Method
- Electron microscopy
- Resolution
- 4.9 Å
- Organism
- Saccharomyces cerevisiae S288C
- Chains
- 8
- Atoms
- 9,689
- Mol. weight
- 302.15 kDa
- Released
- 8 Apr 2026
Explore 9S4Q in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
9S4Q contains 55 α-helices and 26 β-strands across 8 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 24: 2 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 153-168 | 16 | |
| β-strand | 170-173 | 4 | 5 |
| β-strand | 178-182 | 5 | 5 |
| β-strand | 189-193 | 5 | 5 |
| α-helix | 200-212 | 13 | |
Chain 25: 5 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 125-131 | 7 | |
| α-helix | 134-145 | 12 | |
| β-strand | 148-151 | 4 | 6 |
| β-strand | 159-162 | 4 | 6 |
| β-strand | 163 | 1 | 7 |
| β-strand | 169 | 1 | 7 |
| β-strand | 170-173 | 4 | 8 |
| β-strand | 181-185 | 5 | 8 |
| α-helix | 190-198 | 9 | |
| α-helix | 199-203 | 5 | |
| α-helix | 206-220 | 15 | |
Chain Ds: 5 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 435-467 | 33 | |
| α-helix | 471-481 | 11 | |
| α-helix | 487-489 | 3 | |
| α-helix | 493-545 | 53 | |
| α-helix | 559-575 | 17 | |
Chain Kl: 11 helices, 9 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 720-731 | 12 | |
| β-strand | 733-739 | 7 | 2 |
| β-strand | 742-747 | 6 | 2 |
| α-helix | 748-750 | 3 | |
| β-strand | 753-757 | 5 | 2 |
| α-helix | 759-762 | 4 | |
| α-helix | 766-768 | 3 | |
| β-strand | 770-772 | 3 | 2 |
| α-helix | 783-793 | 11 | |
| α-helix | 798-800 | 3 | |
| α-helix | 801-809 | 9 | |
| α-helix | 814-816 | 3 | |
| α-helix | 817-823 | 7 | |
| β-strand | 828-832 | 5 | 4 |
| β-strand | 838-846 | 9 | 4 |
| β-strand | 851-858 | 8 | 4 |
| α-helix | 859-867 | 9 | |
| β-strand | 873-881 | 9 | 4 |
| α-helix | 892-901 | 10 | |
| β-strand | 912-915 | 4 | 4 |
Chain Mt: 14 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 2-4 | 3 | |
| α-helix | 6-16 | 11 | |
| α-helix | 20-48 | 29 | |
| β-strand | 51-52 | 2 | 1 |
| β-strand | 55-56 | 2 | 1 |
| α-helix | 58-86 | 29 | |
| α-helix | 87-91 | 5 | |
| α-helix | 93-95 | 3 | |
| α-helix | 97-100 | 4 | |
| α-helix | 107-109 | 3 | |
| α-helix | 117-168 | 52 | |
| α-helix | 175-184 | 10 | |
| α-helix | 187-208 | 22 | |
| α-helix | 211-218 | 8 | |
| α-helix | 232-247 | 16 | |
| β-strand | 277-278 | 2 | 2 |
| α-helix | 282-288 | 7 | |
Chain Nn: 10 helices, 0 β-strands
| 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 | 116-174 | 59 | |
| α-helix | 177-179 | 3 | |
| α-helix | 186-198 | 13 | |
Chain Ns: 3 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 99-159 | 61 | |
| α-helix | 167-171 | 5 | |
| α-helix | 175-213 | 39 | |
Chain Zw: 5 helices, 5 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 282-288 | 7 | |
| α-helix | 289-293 | 5 | |
| α-helix | 298-300 | 3 | |
| β-strand | 301-307 | 7 | 3 |
| β-strand | 312-317 | 6 | 3 |
| β-strand | 322-327 | 6 | 3 |
| β-strand | 338-345 | 8 | 3 |
| β-strand | 348-351 | 4 | 3 |
| α-helix | 353-363 | 11 | |
| α-helix | 371-384 | 14 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Kinetochore-associated protein NNF1 | Nn | protein | 201 | Saccharomyces cerevisiae S288C | P47149 (AlphaFold model) |
| Kinetochore-associated protein MTW1 | Mt | protein | 289 | Saccharomyces cerevisiae S288C | P39731 (AlphaFold model) |
| Outer kinetochore KNL1 complex subunit KRE28 | Zw | protein | 420 | Saccharomyces cerevisiae S288C | Q04431 (AlphaFold model) |
| Outer kinetochore KNL1 complex subunit SPC105 | Kl | protein | 474 | Saccharomyces cerevisiae S288C | P53148 (AlphaFold model) |
| Kinetochore-associated protein DSN1 | Ds | protein | 576 | Saccharomyces cerevisiae S288C | P40568 |
| Kinetochore protein SPC24 | 24 | protein | 213 | Saccharomyces cerevisiae S288C | Q04477 |
| Kinetochore protein SPC25 | 25 | protein | 221 | Saccharomyces cerevisiae S288C | P40014 |
| Kinetochore-associated protein NSL1 | Ns | protein | 216 | Saccharomyces cerevisiae S288C | Q12143 |
Sequence of entity 1 (Nn), FASTA
>9S4Q_1 Kinetochore-associated protein NNF1 (chains Nn)
MVNSHGIRYIRLKQVFNRALDQSISKLQSWDKVSSCFPQYVNSKQGAINVANCQRQLTEF
WTELCQREFKEIMEERNVEQKLNELDELILEAKERYTDRDQDEVNKGPAIDELSSKELVE
CHLYSQRMHAIHEIDERLAKVNEMNDQLAQELKDLETQVEVEKNEIGKMYDEYLGSHTDQ
PANVLLVQSLNDMVLELKENY
Sequence of entity 2 (Mt), FASTA
>9S4Q_2 Kinetochore-associated protein MTW1 (chains Mt)
MSAPTMRSTSILTEHLGYPPISLVDDIINAVNEIMYKCTAAMEKYLLSKSKIGEEDYGEE
IKSGVAKLESLLENSVDKNFDKLELYVLRNVLRIPEEYLDANVFRLENQKDLVIVDENEL
KKSEEKLREKVNDVELAFKKNEMLLKRVTKVKRLLFTIRGFKQKLNELLKCKDDVQLQKI
LESLKPIDDTMTLLTDSLRKLYVDSESTSSTEEVEALLQRLKTNGKQNNKDFRTRYIDIR
TNNVLRKLGLLGDKEDEKQSAKPDARTQAGDIVSIDIEEPQLDLLDDVL
Sequence of entity 3 (Zw), FASTA
>9S4Q_3 Outer kinetochore KNL1 complex subunit KRE28 (chains Zw)
MDTGSASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVNP
LRNDESLDVEGKEVFVNPKILSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQ
LDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQETGHNFAERQDLINELYLEAT
GDIENCWDSLNELKNLTNKEDKNMMGEKDTILNSSDSDDFVEETYTNWQKLLFLQKQNQR
LTKELKEMHEVKNQIIRKGEQSKKEDSGHLMANESELCQSINLLTKFWEKHFLLKGSKTT
ILNFEIFTQLGKVQFEIKDMQYIIAISLSDLKRPMIKDITILQKAGGNIVTDIEASSKFN
NKYRNNTKVQIFEVMDDIISELTNEENLYFQSWSHPQFEKGGGSGGGSGGGSWSHPQFEK
Sequence of entity 4 (Kl), FASTA
>9S4Q_4 Outer kinetochore KNL1 complex subunit SPC105 (chains Kl)
MSGIALPTQDYTLREFINEVGVGFLDTKLIDDLDKKVNFPLNSFNFVENQRIDNVFSAFY
IDIPILEVEAFRCKELWRSINESKDKFKDFEAQIDKSHPPLLLQEYFSSDEKMKQLMRDQ
LQLVKGYSKLEAAMEWYEWRKKQLNGLELILAENLNTLKREYEKLNEEVEKVNSIRGKIR
KLNEAIKEEIRSLKNLPSDSYKPTLMNRIKIEAFKQELMEHSISLSSSNDFTQEMRSLKL
AIAKKSNDILTLRSEVASIDKKIEKRKLFTRFDLPKLRDTLKILESLTGVRFLKFSKATL
SIAFLQLDDLRVDINLANFKNNPLSSMKVMNDSNNDDMSYHLFTMLLKNVEAEHQDSMLS
NLFFAMKKWRPLLKYIKLLKLLFPVKITQTEEEEALLQFKDYDRRNKTAFFYVISLVSFA
QGVFSENGQIPMKVHISTQQDYSPSREVLSDRITHKISGVLPSFTKSRIHLEFT
Sequence of entity 5 (Ds), FASTA
>9S4Q_5 Kinetochore-associated protein DSN1 (chains Ds)
MSLEPTQTVSGTPPMLHQRTHKQVYPLRMETIPILESDSKATLQSNEPTQKDEEETEYFE
NKQSVSNLSPDLKFKRHKNKHIQGFPTLGERLDNLQDIKKAKRVENFNSSAPIADDNHSG
DATANATANATANATANVNASAMPAPYMPYYYYYHPMNAPTPAMIPYPGSPMHSIMPNSS
LQPFYSQPTAAGGPDMTTPQNISSSQQLLPAPQLFPYGSFHQQQLQQPHYIQRTRERKKS
IGSQRGRRLSMLASQANGGSTIISPHKDIPEEDFYTVVGNASFGKNLQIRQLFNWCLMRS
LHKLELKAKNQEEEGELEHLTKKSKLESTKAETDYVDPKRLAMVIIKEFVDDLKKDHIAI
DWEDEEKYEDEDEEKILDNTENYDDTELRQLFQENDDDDDDDDEVDYSEIQRSRRKFSER
RKALPKEPKKLLPNSKNVENTKNLSILTSKVNAIKNEVKEWAVTLDTSRPDLEWQELTSF
SSQPLEPLSDTEEPDLAIADVETKLETKVDELRYQSHILNSHSLALNEITNSKVNKLNIE
TMRKISSETDDDHSQVINPQQLLKGLSLSFSKKLDL
Sequence of entity 6 (24), FASTA
>9S4Q_6 Kinetochore protein SPC24 (chains 24)
MSQKDNLLDNPVEFLKEVRESFDIQQDVDAMKRIRHDLDVIKEESEARISKEHSKVSESN
KKLNAERINVAKLEGDLEYTNEESNEFGSKDELVKLLKDLDGLERNIVSLRSELDEKMKL
YLKDSEIISTPNGSKIKAKVIEPELEEQSAVTPEANENILKLKLYRSLGVILDLENDQVL
INRKNDGNIDILPLDNNLSDFYKTKYIWERLGK
Sequence of entity 7 (25), FASTA
>9S4Q_7 Kinetochore protein SPC25 (chains 25)
MASIDAFSDLERRMDGFQKDVAQVLARQQNHARQQLQQFQAEMRQLHNQHQHLIDELQRL
ATQRTALQQQIHAAQQATNTTREQWRSYHERESELSRRQSTLAAQSRELDSLLQQRGKEC
VQLRARWAAQSGNDAAEVALYERLLQLRVLPGASDVHDVRFVFGDDSRCWIEVAMHGDHV
IGNSHPALDPKSRATLEHVLTVQGDLAAFLVVARDMLLASL
Sequence of entity 8 (Ns), FASTA
>9S4Q_8 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 P47149 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9S53 6.5 Å, Cryo-EM structure of the base of the Saccharomyces cerevisiae KMN junction complex…
- 9S5N 7.2 Å, Cryo-EM structure of the Saccharomyces cerevisiae KMN junction complex containing the…
Browse structure collections
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