Solution structure of the first Src homology 3 domain of Nck2. Determined by solution NMR. Released 9 May 2006.
Explore 2B86 in 3D Show helices and sheets RCSB PDB PDBe
2B86 contains 1 α-helix 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 |
|---|---|---|---|
| α-helix | 2-4 | 3 | |
| β-strand | 5-9 | 5 | 1 |
| β-strand | 13 | 1 | 2 |
| β-strand | 23 | 1 | 2 |
| β-strand | 28-33 | 6 | 1 |
| β-strand | 40-42 | 3 | 1 |
| β-strand | 48-50 | 3 | 1 |
| β-strand | 56-58 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cytoplasmic protein NCK2 | A | protein | 67 | Homo sapiens | O43639 (AlphaFold model) |
>2B86_1 Cytoplasmic protein NCK2 (chains A) MTEEVIVIAKWDYTAQQDQELDIKKNERLWLLDDSKTWWRVRNAANRTGYVPSNYVERKL EHHHHHH
Solution structure of the first SRC homology 3 domain of human nck2. Park, S., Takeuchi, K., Wagner, G. J Biomol NMR (2006) 34:203-208. DOI 10.1007/s10858-006-0019-5 · PubMed
Other PDB entries of the same protein (UniProt O43639 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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