7L7Q: Ctf3c with Ulp2-KIM

Ctf3c with Ulp2-KIM. Determined by electron microscopy at 3.7 Å resolution. Released 10 Feb 2021.

Method
Electron microscopy
Resolution
3.7 Å
Organism
Saccharomyces cerevisiae
Chains
3
Atoms
5,619
Mol. weight
133.93 kDa
Released
10 Feb 2021

Explore 7L7Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain H: 6 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix4-3835
α-helix47-7125
α-helix83-886
α-helix91-955
α-helix97-10812
α-helix110-13324
Chain I: 22 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix296-3016
α-helix312-3165
α-helix337-34711
α-helix355-36814
α-helix375-38713
α-helix390-40011
α-helix410-42011
α-helix430-44718
α-helix457-47418
α-helix479-49315
α-helix507-52418
α-helix532-5343
α-helix539-5468
α-helix551-56515
α-helix578-58811
α-helix609-6157
α-helix641-65313
α-helix667-6759
α-helix678-6836
α-helix693-70412
α-helix710-7123
α-helix713-72210
Chain K: 2 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix6-3934
α-helix70-12859

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Inner kinetochore subunit MCM16Hprotein184Saccharomyces cerevisiaeQ12262 (AlphaFold model)
Inner kinetochore subunit CTF3Iprotein736Saccharomyces cerevisiaeQ12748 (AlphaFold model)
Inner kinetochore subunit MCM22Kprotein242Saccharomyces cerevisiaeP47167 (AlphaFold model)
Sequence of entity 1 (H), FASTA
>7L7Q_1 Inner kinetochore subunit MCM16 (chains H)
SNAMTNSSEKQWERIQQLEKEHVEVYRELLITLDRLYLIRKHNHAVILSHTQQRLLEIRH
QLQINLEKTALLIRLLEKPDNTNVLFTKLQNLLEESNSLDYELLQSLGAQSSLHKQLIES
RAERDELMSKLIELSSKFPKPTIPPDDSDTAGKQVEVEKENETIQELMIALQIHSGYTNI
SYTI
Sequence of entity 2 (I), FASTA
>7L7Q_2 Inner kinetochore subunit CTF3 (chains I)
SNAMSLILDDIILSLTNANERTPPQALKTTLSLLYEKSKQYGLSSPQLQALVRLLCETSI
IDTVTKVYIVENCFLPDGYLTKELLLEIINHLGTPTVFSRYRIQTPPVLQSALCKWLVHV
YFLFPVHSEREHNISSSIWLHLWQFSFLQKWITPLVIWQATTPVDVKPWKLSIIKRCAMH
PGYRDAPGSATLILQRFQCLVGASSQITESIITINCNRKTLKSHRNLKLDAHFLSILKRI
LSRAHPANFPADTVQNTIDMYLSEIHQLGADSIYPLRLQSLPEYVPSDSTVSLWDVTSLE
QLAQNWPQLHIPNDVDYMMKPSLNSNVLLPRKVMSRDSLKHLYSSIILIKNSRDESSSPY
EWCIWQLKRCFAHQIETPQEVIPIIISVSSMDNKLSSRIIQTFCNLKYLKLDELTLKKVC
GGILPLWKPELISGTREFFVKFMASIFMWSTRDGHDNNCTFSETCFYVLQMITNWVLDDK
LIALGLTLLHDMQSLLTLDKIFNNATSNRFSTMAFISSLDILTQLSKQTKSDYAIQYLIV
GPDIMNKVFSSDDPLLLSAACRYLVATKNKLMQYPSTNKFVRMQNQYIMDLTNYLYRNKV
LSSKSLFGVSPDFFKQILENLYIPTADFKNAKFFTITGIPALSYICIIILRRLETAENTK
IKFTSGIINEETFNNFFRVHHDEIGQHGWIKGVNNIHDLRVKILMHLSNTANPYRDIAAF
LFTYLKSLSKYSVQNS
Sequence of entity 3 (K), FASTA
>7L7Q_3 Inner kinetochore subunit MCM22 (chains K)
SNAMDVEKDVLDVYIKNLENQIGNKRYFLKQAQGAIDEITKRSLDTEGKPVNSEVFTELL
RKPMFFSERADPIGFSLTSNFLSLRAQSSSEWLSLMNDQSVDQKAMLLLQNNINSDLKEL
LRKLQHQMTIMDSKKQDHAHIRTRKARNKELWDSLADFLKGYLVPNLDDNDESIDSLTNE
VMLLMKRLIEHDLNLTLNDFSSKTIPIYRLLLRANIITVIEGSTNPGTKYIKLIDFNETS
LT

Primary citation

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:

Browse structure collections

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