Ctf3c with Ulp2-KIM. Determined by electron microscopy at 3.7 Å resolution. Released 10 Feb 2021.
Explore 7L7Q in 3D Show helices and sheets RCSB PDB PDBe
7L7Q contains 30 α-helices and 0 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 | 4-38 | 35 | |
| α-helix | 47-71 | 25 | |
| α-helix | 83-88 | 6 | |
| α-helix | 91-95 | 5 | |
| α-helix | 97-108 | 12 | |
| α-helix | 110-133 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 296-301 | 6 | |
| α-helix | 312-316 | 5 | |
| α-helix | 337-347 | 11 | |
| α-helix | 355-368 | 14 | |
| α-helix | 375-387 | 13 | |
| α-helix | 390-400 | 11 | |
| α-helix | 410-420 | 11 | |
| α-helix | 430-447 | 18 | |
| α-helix | 457-474 | 18 | |
| α-helix | 479-493 | 15 | |
| α-helix | 507-524 | 18 | |
| α-helix | 532-534 | 3 | |
| α-helix | 539-546 | 8 | |
| α-helix | 551-565 | 15 | |
| α-helix | 578-588 | 11 | |
| α-helix | 609-615 | 7 | |
| α-helix | 641-653 | 13 | |
| α-helix | 667-675 | 9 | |
| α-helix | 678-683 | 6 | |
| α-helix | 693-704 | 12 | |
| α-helix | 710-712 | 3 | |
| α-helix | 713-722 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 6-39 | 34 | |
| α-helix | 70-128 | 59 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Inner kinetochore subunit MCM16 | H | protein | 184 | Saccharomyces cerevisiae | Q12262 (AlphaFold model) |
| Inner kinetochore subunit CTF3 | I | protein | 736 | Saccharomyces cerevisiae | Q12748 (AlphaFold model) |
| Inner kinetochore subunit MCM22 | K | protein | 242 | Saccharomyces cerevisiae | P47167 (AlphaFold model) |
>7L7Q_1 Inner kinetochore subunit MCM16 (chains H) SNAMTNSSEKQWERIQQLEKEHVEVYRELLITLDRLYLIRKHNHAVILSHTQQRLLEIRH QLQINLEKTALLIRLLEKPDNTNVLFTKLQNLLEESNSLDYELLQSLGAQSSLHKQLIES RAERDELMSKLIELSSKFPKPTIPPDDSDTAGKQVEVEKENETIQELMIALQIHSGYTNI SYTI
>7L7Q_2 Inner kinetochore subunit CTF3 (chains I) SNAMSLILDDIILSLTNANERTPPQALKTTLSLLYEKSKQYGLSSPQLQALVRLLCETSI IDTVTKVYIVENCFLPDGYLTKELLLEIINHLGTPTVFSRYRIQTPPVLQSALCKWLVHV YFLFPVHSEREHNISSSIWLHLWQFSFLQKWITPLVIWQATTPVDVKPWKLSIIKRCAMH PGYRDAPGSATLILQRFQCLVGASSQITESIITINCNRKTLKSHRNLKLDAHFLSILKRI LSRAHPANFPADTVQNTIDMYLSEIHQLGADSIYPLRLQSLPEYVPSDSTVSLWDVTSLE QLAQNWPQLHIPNDVDYMMKPSLNSNVLLPRKVMSRDSLKHLYSSIILIKNSRDESSSPY EWCIWQLKRCFAHQIETPQEVIPIIISVSSMDNKLSSRIIQTFCNLKYLKLDELTLKKVC GGILPLWKPELISGTREFFVKFMASIFMWSTRDGHDNNCTFSETCFYVLQMITNWVLDDK LIALGLTLLHDMQSLLTLDKIFNNATSNRFSTMAFISSLDILTQLSKQTKSDYAIQYLIV GPDIMNKVFSSDDPLLLSAACRYLVATKNKLMQYPSTNKFVRMQNQYIMDLTNYLYRNKV LSSKSLFGVSPDFFKQILENLYIPTADFKNAKFFTITGIPALSYICIIILRRLETAENTK IKFTSGIINEETFNNFFRVHHDEIGQHGWIKGVNNIHDLRVKILMHLSNTANPYRDIAAF LFTYLKSLSKYSVQNS
>7L7Q_3 Inner kinetochore subunit MCM22 (chains K) SNAMDVEKDVLDVYIKNLENQIGNKRYFLKQAQGAIDEITKRSLDTEGKPVNSEVFTELL RKPMFFSERADPIGFSLTSNFLSLRAQSSSEWLSLMNDQSVDQKAMLLLQNNINSDLKEL LRKLQHQMTIMDSKKQDHAHIRTRKARNKELWDSLADFLKGYLVPNLDDNDESIDSLTNE VMLLMKRLIEHDLNLTLNDFSSKTIPIYRLLLRANIITVIEGSTNPGTKYIKLIDFNETS LT
Ctf3/CENP-I provides a docking site for the desumoylase Ulp2 at the kinetochore. Quan, Y., Hinshaw, S.M., Wang, P.C. et al. J Cell Biol (2021) 220. DOI 10.1083/jcb.202012149 · PubMed
Other PDB entries of the same protein (UniProt Q12262 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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