2N64: C-terminal Coiled-Coil Domain of CIN85

NMR Structure of the C-terminal Coiled-Coil Domain of CIN85. Determined by solution NMR. Released 13 Jul 2016.

Method

Solution NMR

Organism

Homo sapiens

Chains

3

Atoms

1,827

Mol. weight

26.29 kDa

Released

13 Jul 2016

Explore 2N64 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A, B and C: 1 helix, 0 β-strands

Molecules and chains

>2N64_1 SH3 domain-containing kinase-binding protein 1 (chains A, B, C)
GHMEGKPKMEPAASSQAAVEELRTQVRELRSIIETMKDQQKREIKQLLSELDEEKKIRLR
LQMEVNDIKKALQSK

Primary citation

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

Related structures

Other PDB entries of the same protein (UniProt Q96B97 (AlphaFold model), which also has an AlphaFold model), best resolution first:

• 5ABS 1.74 Å, Crystal structure of the C-terminal coiled-coil domain of CIN85 in space group P321
• 2BZ8 2.0 Å, N-terminal Sh3 domain of CIN85 bound to Cbl-b peptide
• 2YDL 2.05 Å, Crystal structure of SH3C from CIN85
• 2K6D CIN85 Sh3-C domain in complex with ubiquitin
• 2K9G Solution structure of the third SH3 domain of the Cin85 adapter protein
• 2O2O Solution structure of domain B from human CIN85 PROTEIN

Browse structure collections

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