NMR Structure of the C-terminal Coiled-Coil Domain of CIN85. Determined by solution NMR. Released 13 Jul 2016.
Explore 2N64 in 3D Show helices and sheets RCSB PDB PDBe
2N64 contains 3 α-helices and 0 β-strands across 3 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 | 605-663 | 59 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| SH3 domain-containing kinase-binding protein 1 | A, B, C | protein | 75 | Homo sapiens | Q96B97 (AlphaFold model) |
>2N64_1 SH3 domain-containing kinase-binding protein 1 (chains A, B, C) GHMEGKPKMEPAASSQAAVEELRTQVRELRSIIETMKDQQKREIKQLLSELDEEKKIRLR LQMEVNDIKKALQSK
The adaptor protein CIN85 assembles intracellular signaling clusters for B cell activation. Kuhn, J., Wong, L.E., Pirkuliyeva, S. et al. Sci Signal (2016) 9:ra66-ra66. DOI 10.1126/scisignal.aad6275 · PubMed
Other PDB entries of the same protein (UniProt Q96B97 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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