6WUC: The yeast Ctf3 complex with Cnn1-Wip1

The yeast Ctf3 complex with Cnn1-Wip1. Determined by electron microscopy at 3.23 Å resolution. Released 17 Jun 2020.

Method: Electron microscopy
Resolution: 3.23 Å
Organism: Saccharomyces cerevisiae
Chains: 5
Atoms: 10,284
Mol. weight: 185.82 kDa
Released: 17 Jun 2020

Explore 6WUC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6WUC contains 70 α-helices and 8 β-strands across 5 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: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	4-38	35
α-helix	47-65	19
α-helix	68-71	4
α-helix	83-93	11
α-helix	97-105	9
α-helix	110-133	24
α-helix	137-141	5
α-helix	148-155	8
α-helix	157-172	16

Chain I: 43 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	1-13	13
α-helix	23-35	13
α-helix	42-54	13
α-helix	60-69	10
α-helix	79-86	8
α-helix	94-96	3
α-helix	100-103	4
α-helix	104-116	13
α-helix	118-120	3
α-helix	121-124	4
α-helix	128-138	11
α-helix	139-141	3
α-helix	144-146	3
α-helix	149-156	8
α-helix	160-162	3
α-helix	165-175	11
α-helix	178-180	3
α-helix	184-198	15
α-helix	202-208	7
α-helix	219-222	4
α-helix	228-241	14
α-helix	248-264	17
β-strand	289	1	1
α-helix	296-301	6
β-strand	307	1	1
α-helix	312-315	4
α-helix	355-368	14
α-helix	375-386	12
α-helix	390-400	11
α-helix	404-408	5
α-helix	410-420	11
α-helix	432-447	16
α-helix	458-474	17
α-helix	479-490	12
α-helix	512-524	13
α-helix	532-534	3
α-helix	542-546	5
α-helix	551-562	12
α-helix	576-588	13
α-helix	608-614	7
α-helix	640-654	15
α-helix	667-676	10
α-helix	678-683	6
α-helix	693-704	12
α-helix	712-722	11

Chain K: 9 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	7-38	32
α-helix	47-49	3
α-helix	53-56	4
α-helix	70-128	59
α-helix	141-155	15
α-helix	156-160	5
α-helix	171-186	16
β-strand	193	1	2
α-helix	194-196	3
α-helix	202-210	9
β-strand	214-215	2	3
β-strand	218	1	4
β-strand	226	1	4
β-strand	227	1	2
β-strand	229-230	2	3

Chain T: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	276-281	6
α-helix	283-286	4
α-helix	297-316	20
α-helix	324-331	8
α-helix	337-347	11
α-helix	350-360	11

Chain W: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	16-21	6
α-helix	37-67	31
α-helix	79-82	4

Molecules and chains

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)
Inner kinetochore subunit WIP1	W	protein	92	Saccharomyces cerevisiae	Q2V2P8 (AlphaFold model)
Inner kinetochore subunit CNN1	T	protein	361	Saccharomyces cerevisiae	P43618

Sequence of entity 1 (H), FASTA

>6WUC_1 Inner kinetochore subunit MCM16 (chains H)
SNAMTNSSEKQWERIQQLEKEHVEVYRELLITLDRLYLIRKHNHAVILSHTQQRLLEIRH
QLQINLEKTALLIRLLEKPDNTNVLFTKLQNLLEESNSLDYELLQSLGAQSSLHKQLIES
RAERDELMSKLIELSSKFPKPTIPPDDSDTAGKQVEVEKENETIQELMIALQIHSGYTNI
SYTI

Sequence of entity 2 (I), FASTA

>6WUC_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

>6WUC_3 Inner kinetochore subunit MCM22 (chains K)
SNAMDVEKDVLDVYIKNLENQIGNKRYFLKQAQGAIDEITKRSLDTEGKPVNSEVFTELL
RKPMFFSERADPIGFSLTSNFLSLRAQSSSEWLSLMNDQSVDQKAMLLLQNNINSDLKEL
LRKLQHQMTIMDSKKQDHAHIRTRKARNKELWDSLADFLKGYLVPNLDDNDESIDSLTNE
VMLLMKRLIEHDLNLTLNDFSSKTIPIYRLLLRANIITVIEGSTNPGTKYIKLIDFNETS
LT

Sequence of entity 4 (W), FASTA

>6WUC_4 Inner kinetochore subunit WIP1 (chains W)
SNAMDTEALANYLLRQLSLDAEENKLEDLLQRQNEDQESSQEYNKKLLLACGFQAILRKI
LLDARTRATAEGLREVYPYHIEAATQAFLDSQ

Sequence of entity 5 (T), FASTA

>6WUC_5 Inner kinetochore subunit CNN1 (chains T)
MSTPRKAAGNNENTEVSEIRTPFRERALEEQRLKDEVLIRNTPGYRKLLSASTKSHDILN
KDPNEVRSFLQDLSQVLARKSQGNDTTTNKTQARNLIDELAYEESQPEENELLRSRSEKL
TDNNIGNETQPDYTSLSQTVFAKLQERDKGLKSRKIDPIIIQDVPTTGHEDELTVHSPDK
ANSISMEVLRTSPSIGMDQVDEPPVRDPVPISITQQEEPLSEDLPSDDKEETEEAENEDY
SFENTSDENLDDIGNDPIRLNVPAVRRSSIKPLQIMDLKHLTRQFLNENRIILPKQTWST
IQEESLNIMDFLKQKIGTLQKQELVDSFIDMGIINNVDDMFELAHELLPLELQSRIESYL
F

Primary citation

The Structural Basis for Kinetochore Stabilization by Cnn1/CENP-T. Hinshaw, S.M., Harrison, S.C. Curr Biol (2020) 30:3425-3431.e3. DOI 10.1016/j.cub.2020.06.024 · PubMed

Other PDB entries of the same protein (UniProt Q12262 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6YPC 2.9 Å, Crystal structure of the kinetochore subunits H/I/K/T/W penta-complex from S. cerevisiae…
10FI 3.3 Å, apo CCAN purified from budding yeast
8OVW 3.4 Å, Cryo-EM structure of CBF1-CCAN bound topologically to centromeric DNA
8OW0 3.4 Å, Cryo-EM structure of CBF1-CCAN bound topologically to a centromeric CENP-A nucleosome
6QLE 3.55 Å, Structure of inner kinetochore CCAN complex
7L7Q 3.7 Å, Ctf3c with Ulp2-KIM
8OW1 3.7 Å, Cryo-EM structure of the yeast Inner kinetochore bound to a CENP-A nucleosome.
10DQ 3.9 Å, Cbf1-CCAN-CEN complex
6QLD 4.15 Å, Structure of inner kinetochore CCAN-Cenp-A complex
6OUA 4.18 Å, Cryo-EM structure of the yeast Ctf3 complex
10JC 6.5 Å, CCAN dimer purified from budding yeast

Browse structure collections

About this viewer

MolViewer shows 6WUC 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.