2KDD: Borealin

Solution structure of the conserved C-terminal dimerization domain of Borealin. Determined by solution NMR. Released 30 Jun 2009.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
872
Mol. weight
16.16 kDa
Released
30 Jun 2009

Explore 2KDD in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A and B: 3 helices, 2 β-strands

ElementResiduesLengthSheet
β-strand228-22921
α-helix238-2392
β-strand241-24221
α-helix248-2525
α-helix256-27520

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
BorealinA, Bprotein76Homo sapiensQ53HL2 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2KDD_1 Borealin (chains A, B)
GSAGERIYNISGNGSPLADSKEIFLTVPVGGGESLRLLASDLQRHSIAQLDPEALGNIKK
LSNRLAQICSSIRTHK

Primary citation

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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