Crystal Structure of swapped human Nck SH3.1 domain, 1.3A, orthorhombic form III. Determined by X-ray diffraction at 1.27 Å resolution. Released 12 Feb 2020.
Explore 5QU7 in 3D Show helices and sheets RCSB PDB PDBe
5QU7 contains 2 α-helices and 16 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 6-10 | 5 | 1 |
| β-strand | 14 | 1 | 2 |
| β-strand | 21 | 1 | 1 |
| β-strand | 24 | 1 | 2 |
| β-strand | 29-33 | 5 | 1 |
| β-strand | 39-43 | 5 | 1 |
| β-strand | 49-53 | 5 | 1 |
| α-helix | 54-56 | 3 | |
| β-strand | 57-59 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cytoplasmic protein NCK1 | A, B | protein | 82 | Homo sapiens | P16333 (AlphaFold model) |
>5QU7_1 Cytoplasmic protein NCK1 (chains A, B) SGGLNDIFEAQKIEWHEGSENLYFQSEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKS WWRVRNSMNKTGFVPSNYVERK
Small molecule AX-024 reduces T cell proliferation independently of CD3ε/Nck1 interaction, which is governed by a domain swap in the Nck1-SH3.1 domain. Richter, K., Rufer, A.C., Muller, M. et al. J Biol Chem (2020) 295:7849-7864. DOI 10.1074/jbc.RA120.012788 · 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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