Structure of the Knl1/Nsl1 complex. Determined by X-ray diffraction at 2.8 Å resolution. Released 19 Mar 2014.
Explore 4NF9 in 3D Show helices and sheets RCSB PDB PDBe
4NF9 contains 24 α-helices and 24 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 | 2097-2104 | 8 | |
| β-strand | 2109-2114 | 6 | 1 |
| β-strand | 2118-2123 | 6 | 1 |
| β-strand | 2128-2134 | 7 | 1 |
| α-helix | 2135-2136 | 2 | |
| α-helix | 2141-2143 | 3 | |
| α-helix | 2146-2148 | 3 | |
| β-strand | 2150 | 1 | 2 |
| β-strand | 2151-2158 | 8 | 1 |
| β-strand | 2160 | 1 | 3 |
| α-helix | 2167-2182 | 16 | |
| α-helix | 2184-2186 | 3 | |
| β-strand | 2192 | 1 | 2 |
| α-helix | 2193-2195 | 3 | |
| α-helix | 2196-2223 | 28 | |
| α-helix | 2224-2227 | 4 | |
| β-strand | 2229-2235 | 7 | 4 |
| β-strand | 2238-2245 | 8 | 4 |
| β-strand | 2250-2257 | 8 | 4 |
| α-helix | 2266-2268 | 3 | |
| β-strand | 2269-2275 | 7 | 4 |
| α-helix | 2280-2287 | 8 | |
| α-helix | 2296-2307 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2110-2114 | 5 | 5 |
| β-strand | 2118-2123 | 6 | 5 |
| β-strand | 2128-2134 | 7 | 5 |
| α-helix | 2135-2136 | 2 | |
| α-helix | 2140 | 1 | |
| α-helix | 2146-2148 | 3 | |
| β-strand | 2150 | 1 | 6 |
| β-strand | 2151-2158 | 8 | 5 |
| β-strand | 2160 | 1 | 7 |
| α-helix | 2167-2183 | 17 | |
| α-helix | 2184-2186 | 3 | |
| β-strand | 2192 | 1 | 6 |
| α-helix | 2196-2223 | 28 | |
| α-helix | 2224-2227 | 4 | |
| β-strand | 2229-2235 | 7 | 8 |
| β-strand | 2238-2245 | 8 | 8 |
| β-strand | 2250-2257 | 8 | 8 |
| α-helix | 2266-2268 | 3 | |
| β-strand | 2269-2275 | 7 | 8 |
| α-helix | 2280-2287 | 8 | |
| α-helix | 2296-2308 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 272 | 1 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 271 | 1 | |
| β-strand | 272 | 1 | 7 |
| α-helix | 273 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein CASC5 | A, B | protein | 221 | Homo sapiens | Q8NG31 (AlphaFold model) |
| Kinetochore-associated protein NSL1 homolog | C, D | protein | 26 | Homo sapiens | Q96IY1 (AlphaFold model) |
>4NF9_1 Protein CASC5 (chains A, B) QKQRNRTEELLDQLSLSEWDVVEWSDDQAVFTFVYDTIQLTITFEESVVGFPFLDKRYRK IVDVNFQSLLDEDQAPPSSLLVHKLIFQYVEEKESWKKTCTTQHQLPKMLEEFSLVVHHC RLLGEEIEYLKRWGPNYNLMNIDINNNELRLLFSSSAAFAKFEITLFLSAYYPSVPLPST IQNHVGNTSQDDIATILSKVPLENNYLKNVVKQIYQDLFQD
>4NF9_2 Kinetochore-associated protein NSL1 homolog (chains C, D) LKRKQTKDCPQRKWYPLRPKKINLDT
Modular Assembly of RWD Domains on the Mis12 Complex Underlies Outer Kinetochore Organization. Petrovic, A., Mosalaganti, S., Keller, J. et al. Mol Cell (2014) 53:591-605. DOI 10.1016/j.molcel.2014.01.019 · PubMed
Other PDB entries of the same protein (UniProt Q8NG31 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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