NMR solution structure of the N-terminal SH3 domain of human Nckalpha. Determined by solution NMR. Released 26 Aug 2008.
Explore 2JW4 in 3D Show helices and sheets RCSB PDB PDBe
2JW4 contains 0 α-helices and 5 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 | 31-36 | 6 | 1 |
| β-strand | 42-45 | 4 | 1 |
| β-strand | 51-54 | 4 | 1 |
| β-strand | 60-61 | 2 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cytoplasmic protein NCK1 | A | protein | 72 | Homo sapiens | P16333 (AlphaFold model) |
>2JW4_1 Cytoplasmic protein NCK1 (chains A) GSTMAEEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKSWWRVRNSMNKTGFVPSNYVE RKNSARAAANSS
Interaction between the N-terminal SH3 domain of Nckalpha and CD3epsilon-derived peptides: Non-canonical and canonical recognition motifs. Santiveri, C.M., Borroto, A., Simon, L. et al. Biochim Biophys Acta Proteins Proteom (2009) 1794:110-117. DOI 10.1016/j.bbapap.2008.09.016 · 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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