Solution structure of the conserved C-terminal dimerization domain of Borealin. Determined by solution NMR. Released 30 Jun 2009.
Explore 2KDD in 3D Show helices and sheets RCSB PDB PDBe
2KDD contains 6 α-helices and 4 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 228-229 | 2 | 1 |
| α-helix | 238-239 | 2 | |
| β-strand | 241-242 | 2 | 1 |
| α-helix | 248-252 | 5 | |
| α-helix | 256-275 | 20 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Borealin | A, B | protein | 76 | Homo sapiens | Q53HL2 (AlphaFold model) |
>2KDD_1 Borealin (chains A, B) GSAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKK LSNRLAQICSSIRTHK
Phosphorylation of a borealin dimerization domain is required for proper chromosome segregation. Bourhis, E., Lingel, A., Phung, Q. et al. Biochemistry (2009) 48:6783-6793. DOI 10.1021/bi900530v · PubMed
Other PDB entries of the same protein (UniProt Q53HL2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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