Solution structure of first SH3 domain of adaptor Nck. Determined by solution NMR. Released 26 Feb 2008.
Explore 2JS2 in 3D Show helices and sheets RCSB PDB PDBe
2JS2 contains 0 α-helices and 7 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 | 8-11 | 4 | 1 |
| β-strand | 15 | 1 | 2 |
| β-strand | 25 | 1 | 2 |
| β-strand | 30-35 | 6 | 1 |
| β-strand | 41-44 | 4 | 1 |
| β-strand | 50-53 | 4 | 1 |
| β-strand | 58-60 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cytoplasmic protein NCK1 | A | protein | 63 | Homo sapiens | P16333 (AlphaFold model) |
>2JS2_1 Cytoplasmic protein NCK1 (chains A) GSMAEEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKSWWRVRNSMNKTGFVPSNYVER KNS
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:
MolViewer shows 2JS2 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.