Structure of a Saccharomyces cerevisiae Mps1 peptide bound to dwarf Ndc80 Complex. Determined by X-ray diffraction at 3.02 Å resolution. Released 15 May 2024.
Explore 8V10 in 3D Show helices and sheets RCSB PDB PDBe
8V10 contains 29 α-helices and 7 β-strands across 4 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 | 122-138 | 17 | |
| α-helix | 141-145 | 5 | |
| α-helix | 151-155 | 5 | |
| α-helix | 159-173 | 15 | |
| α-helix | 184-193 | 10 | |
| α-helix | 204-207 | 4 | |
| α-helix | 215-245 | 31 | |
| α-helix | 250-254 | 5 | |
| α-helix | 257-258 | 2 | |
| α-helix | 261-291 | 31 | |
| α-helix | 298-680 | 81 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 166-168 | 3 | |
| α-helix | 1013-1022 | 10 | |
| α-helix | 1031-1034 | 4 | |
| α-helix | 1038-1048 | 11 | |
| α-helix | 1049-1053 | 5 | |
| α-helix | 1057-1064 | 8 | |
| α-helix | 1075-1101 | 27 | |
| α-helix | 1109-1112 | 4 | |
| α-helix | 1116-1136 | 21 | |
| α-helix | 1141-1449 | 56 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 11-20 | 10 | |
| α-helix | 25-53 | 29 | |
| β-strand | 57-60 | 4 | 1 |
| β-strand | 65-69 | 5 | 1 |
| β-strand | 76-80 | 5 | 1 |
| α-helix | 87-94 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-6 | 3 | |
| α-helix | 7-24 | 18 | |
| α-helix | 32-38 | 7 | |
| β-strand | 41-45 | 5 | 2 |
| β-strand | 53-57 | 5 | 2 |
| β-strand | 63-67 | 5 | 2 |
| β-strand | 75-78 | 4 | 2 |
| α-helix | 84-95 | 12 | |
| α-helix | 100-113 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kinetochore protein NDC80 | A | protein | 279 | Saccharomyces cerevisiae | P40460 (AlphaFold model) |
| Mps1/NUF2 chimera protein | B | protein | 233 | Saccharomyces cerevisiae | P33895 (AlphaFold model), P54199 (AlphaFold model) |
| Kinetochore protein SPC24 | C | protein | 100 | Saccharomyces cerevisiae | Q04477 (AlphaFold model) |
| Kinetochore protein SPC25 | D | protein | 115 | Saccharomyces cerevisiae | P40014 |
>8V10_1 Kinetochore protein NDC80 (chains A) SNARDPRPLRDKNFQSAIQEEIYDYLKKNKFDIETNHPISIKFLKQPTQKGFIIIFKWLY LRLDPGYGFTKSIENEIYQILKNLRYPFLESINKSQISAVGGSNWHKFLGMLHWMVRTNI KLDMCLNKVDRSLINQNTQEITILSQPLKTLDEQDQRQERYELMVEKLLIDYFTESYKSF LKLEDNYEPSMQELKLGFEKFVHIINTDVTSTELKLEELKVDLNRKRYKLHQQVIHVIDI TSKFKINIQSSLENSENELGNVIEELRNLEFETEHNVTN
>8V10_2 Mps1/NUF2 chimera protein (chains B) MRQNMKEDITAKYAERRSKRFLISNRTTKLGPAKRASRNQDVFPILDLQELVICLQSCDF ALATQENISRPTSDYMVTLYKQIIENFMGISVESLLNSSNQETGDGHLQEENENIYLDTL NVLVLNKICFKFFENIGVQDFNMTDLYKPEAQRTQRLLSAVVNYARFREERMFDCNSFIL QMESLLGQINKLNDEIKQLQKDFEVEVKEIEIEYSLLSGHINKYMNEMLEYMQ
>8V10_3 Kinetochore protein SPC24 (chains C) MSQKDNLLDNPVEFLKEVRESFDIQQDVDAMKRIRHDLDVIKEESEARLKLYRSLGVILD LENDQVLINRKNDGNIDILPLDNNLSDFYKTKYIWERLGK
>8V10_4 Kinetochore protein SPC25 (chains D) MASIDAFSDLERRMDGFQKDVAQVLARQQNHVALYERLLQLRVLPGASDVHDVRFVFGDD SRCWIEVAMHGDHVIGNSHPALDPKSRATLEHVLTVQGDLAAFLVVARDMLLASL
| ID | Name | Formula | Copies |
|---|---|---|---|
| NI | Nickel (II) ion | Ni | 1 |
A communication hub for phosphoregulation of kinetochore-microtubule attachment. Zahm, J.A., Harrison, S.C. Curr Biol (2024) 34:2308-2318.e6. DOI 10.1016/j.cub.2024.04.067 · PubMed
Other PDB entries of the same protein (UniProt P40460 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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