Solution NMR structure of the GRB2 N-terminal SH3 domain complexed with a ten-residue peptide derived from sos direct refinement against noes, J-couplings, and 1H and 13C chemical shifts, minimized average structure. Determined by solution NMR. Released 4 Sept 1997.
Explore 3GBQ in 3D Show helices and sheets RCSB PDB PDBe
3GBQ contains 2 α-helices and 8 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 | 2-5 | 4 | 1 |
| β-strand | 9 | 1 | 2 |
| β-strand | 16 | 1 | 1 |
| β-strand | 19 | 1 | 2 |
| β-strand | 24-27 | 4 | 1 |
| β-strand | 36-41 | 6 | 1 |
| β-strand | 44-49 | 6 | 1 |
| α-helix | 50-52 | 3 | |
| β-strand | 53-56 | 4 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 2-6 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| GRB2 | A | protein | 74 | Mus musculus | Q60631 (AlphaFold model) |
| SOS-1 | B | protein | 12 | Mus musculus | Q62245 (AlphaFold model) |
>3GBQ_1 GRB2 (chains A) GSRRASVGSMEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKN YIEMKPHPEFIVTD
>3GBQ_2 SOS-1 (chains B) XVPPPVPPRRRX
Solution structure of the Grb2 N-terminal SH3 domain complexed with a ten-residue peptide derived from SOS: direct refinement against NOEs, J-couplings and 1H and 13C chemical shifts. Wittekind, M., Mapelli, C., Lee, V. et al. J Mol Biol (1997) 267:933-952. DOI 10.1006/jmbi.1996.0886 · PubMed
Other PDB entries of the same protein (UniProt Q60631 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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