Crystal structure of the kinetochore subunits H/I/K/T/W penta-complex from S. cerevisiae at 2.9 angstroms. Determined by X-ray diffraction at 2.9 Å resolution. Released 16 Sept 2020.
Explore 6YPC in 3D Show helices and sheets RCSB PDB PDBe
6YPC contains 34 α-helices and 5 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 151-171 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-14 | 11 | |
| α-helix | 21-38 | 18 | |
| β-strand | 40 | 1 | 2 |
| α-helix | 42-54 | 13 | |
| α-helix | 60-70 | 11 | |
| β-strand | 73 | 1 | 2 |
| α-helix | 77-78 | 2 | |
| α-helix | 79-86 | 8 | |
| α-helix | 104-116 | 13 | |
| α-helix | 118-120 | 3 | |
| α-helix | 121-125 | 5 | |
| α-helix | 126-140 | 15 | |
| α-helix | 143-145 | 3 | |
| α-helix | 146-156 | 11 | |
| α-helix | 165-176 | 12 | |
| α-helix | 183-198 | 16 | |
| α-helix | 202-210 | 9 | |
| α-helix | 217-222 | 6 | |
| α-helix | 228-240 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 139-155 | 17 | |
| α-helix | 156-160 | 5 | |
| α-helix | 171-186 | 16 | |
| β-strand | 193 | 1 | 1 |
| α-helix | 194-196 | 3 | |
| α-helix | 202-211 | 10 | |
| β-strand | 214-217 | 4 | 1 |
| β-strand | 227-230 | 4 | 1 |
| α-helix | 231-232 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 273-274 | 2 | |
| α-helix | 275-281 | 7 | |
| α-helix | 283-288 | 6 | |
| α-helix | 295-315 | 21 | |
| α-helix | 323-330 | 8 | |
| α-helix | 337-347 | 11 | |
| α-helix | 350-359 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-14 | 12 | |
| α-helix | 37-67 | 31 | |
| α-helix | 75-88 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Inner kinetochore subunit MCM22 | K | protein | 110 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P47167 (AlphaFold model) |
| Inner kinetochore subunit MCM16 | H | protein | 46 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q12262 (AlphaFold model) |
| Inner kinetochore subunit CNN1 | T | protein | 367 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | P43618 (AlphaFold model) |
| Inner kinetochore subunit WIP1 | W | protein | 89 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q2V2P8 (AlphaFold model) |
| Inner kinetochore subunit CTF3 | I | protein | 251 | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) | Q12748 |
>6YPC_1 Inner kinetochore subunit MCM22 (chains K) MKKQDHAHIRTRKARNKELWDSLADFLKGYLVPNLDDNDESIDSLTNEVMLLMKRLIEHD LNLTLNDFSSKTIPIYRLLLRANIITVIEGSTNPGTKYIKLIDFNETSLT
>6YPC_2 Inner kinetochore subunit MCM16 (chains H) MKPTIPPDDSDTAGKQVEVEKENETIQELMIALQIHSGYTNISYTI
>6YPC_3 Inner kinetochore subunit CNN1 (chains T) MSTPRKAAGNNENTEVSEIRTPFRERALEEQRLKDEVLIRNTPGYRKLLSASTKSHDILN KDPNEVRSFLQDLSQVLARKSQGNDTTTNKTQARNLIDELAYEESQPEENELLRSRSEKL TDNNIGNETQPDYTSLSQTVFAKLQERDKGLKSRKIDPIIIQDVPTTGHEDELTVHSPDK ANSISMEVLRTSPSIGMDQVDEPPVRDPVPISITQQEEPLSEDLPSDDKEETEEAENEDY SFENTSDENLDDIGNDPIRLNVPAVRRSSIKPLQIMDLKHLTRQFLNENRIILPKQTWST IQEESLNIMDFLKQKIGTLQKQELVDSFIDMGIINNVDDMFELAHELLPLELQSRIESYL FENLYFQ
>6YPC_4 Inner kinetochore subunit WIP1 (chains W) MDTEALANYLLRQLSLDAEENKLEDLLQRQNEDQESSQEYNKKLLLACGFQAILRKILLD ARTRATAEGLREVYPYHIEAATQAFLDSQ
>6YPC_5 Inner kinetochore subunit CTF3 (chains I) MSLILDDIILSLTNANERTPPQALKTTLSLLYEKSKQYGLSSPQLQALVRLLCETSIIDT VTKVYIVENCFLPDGYLTKELLLEIINHLGTPTVFSRYRIQTPPVLQSALCKWLVHVYFL FPVHSEREHNISSSIWLHLWQFSFLQKWITPLVIWQATTPVDVKPWKLSIIKRCAMHPGY RDAPGSATLILQRFQCLVGASSQITESIITINCNRKTLKSHRNLKLDAHFLSILKRILSR AHPANENLYFQ
Crystal structure of the Cenp-HIKHead-TW sub-module of the inner kinetochore CCAN complex. Zhang, Z., Bellini, D., Barford, D. Nucleic Acids Res (2020) 48:11172-11184. DOI 10.1093/nar/gkaa772 · PubMed
Other PDB entries of the same protein (UniProt P47167 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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