Crystal Structure of Iml3 from S. cerevisiae. Determined by X-ray diffraction at 2.5 Å resolution. Released 16 Oct 2013.
Explore 4IT3 in 3D Show helices and sheets RCSB PDB PDBe
4IT3 contains 11 α-helices and 13 β-strands across 1 chain. 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 |
|---|---|---|---|
| β-strand | 3-10 | 8 | 1 |
| α-helix | 16-18 | 3 | |
| α-helix | 20-27 | 8 | |
| β-strand | 32-39 | 8 | 1 |
| β-strand | 52-59 | 8 | 1 |
| β-strand | 72-77 | 6 | 1 |
| β-strand | 85-90 | 6 | 1 |
| α-helix | 95-107 | 13 | |
| β-strand | 111-113 | 3 | 1 |
| α-helix | 118-127 | 10 | |
| β-strand | 130-132 | 3 | 2 |
| β-strand | 138-140 | 3 | 2 |
| β-strand | 145-149 | 5 | 1 |
| β-strand | 161-165 | 5 | 1 |
| α-helix | 167-175 | 9 | |
| α-helix | 183 | 1 | |
| α-helix | 184-188 | 5 | |
| α-helix | 189-191 | 3 | |
| α-helix | 192-196 | 5 | |
| α-helix | 200-202 | 3 | |
| β-strand | 205-210 | 6 | 1 |
| β-strand | 214-217 | 4 | 1 |
| β-strand | 221-223 | 3 | 1 |
| α-helix | 230-239 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Central kinetochore subunit IML3 | A | protein | 248 | Saccharomyces cerevisiae | P38265 (AlphaFold model) |
>4IT3_1 Central kinetochore subunit IML3 (chains A) SNAMPYTWKFLGISKQLSLENGIAKLNQLLNLEVDLDIQTIRVPSDPDGGTAADEYIRYE MRLDISNLDEGTYSKFIFLGNSKMEVPMFLCYCGTDNRNEVVLQWLKAEYGVIMWPIKFE QKTMIKLADASIVHVTKENIEQITWFSSKLYFEPETQDKNLRQFSIEIPRESCEGLALGY GNTMHPYNDAIVPYIYNETGMAVERLPLTSVILAGHTKIMRESIVTSTRSLRNRVLAVVL QSIQFTSE
An iml3-chl4 heterodimer links the core centromere to factors required for accurate chromosome segregation. Hinshaw, S.M., Harrison, S.C. Cell Rep (2013) 5:29-36. DOI 10.1016/j.celrep.2013.08.036 · PubMed
Other PDB entries of the same protein (UniProt P38265 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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