Solution structure of second SH3 domain of adaptor Nck. Determined by solution NMR. Released 26 Feb 2008.
Explore 2JS0 in 3D Show helices and sheets RCSB PDB PDBe
2JS0 contains 1 α-helix and 8 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 | 5-9 | 5 | 1 |
| β-strand | 13 | 1 | 2 |
| β-strand | 20 | 1 | 1 |
| β-strand | 23 | 1 | 2 |
| β-strand | 28-34 | 7 | 1 |
| β-strand | 39-44 | 6 | 1 |
| β-strand | 47-52 | 6 | 1 |
| α-helix | 53-55 | 3 | |
| β-strand | 56-57 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cytoplasmic protein NCK1 | A | protein | 61 | Homo sapiens | P16333 (AlphaFold model) |
>2JS0_1 Cytoplasmic protein NCK1 (chains A) GSLNMPAYVKFNYMAEREDELSLIKGTKVIVMEKCSDGWWRGSYNGQVGWFPSNYVTEEG D
Specificity determinants of a novel Nck interaction with the juxtamembrane domain of the epidermal growth factor receptor. Hake, M.J., Choowongkomon, K., Kostenko, O. et al. Biochemistry (2008) 47:3096-3108. DOI 10.1021/bi701549a · PubMed
Other PDB entries of the same protein (UniProt P16333 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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