Gbeta1 stabilization by in vitro evolution and computational design. Determined by X-ray diffraction at 1.7 Å resolution. Released 8 Jan 2008.
Explore 2ONQ in 3D Show helices and sheets RCSB PDB PDBe
2ONQ contains 1 α-helix and 4 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 | 2-8 | 7 | 1 |
| β-strand | 13-19 | 7 | 1 |
| α-helix | 23-36 | 14 | |
| β-strand | 42-46 | 5 | 1 |
| β-strand | 51-55 | 5 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Immunoglobulin G-binding protein G | A | protein | 56 | Streptococcus sp. | P19909 (AlphaFold model) |
>2ONQ_1 Immunoglobulin G-binding protein G (chains A) MQFKLIINGKTLKGEITIEAVDAAEAEKFFKQYANDNGIDGEWTYDDATKTFTVTE
Optimization of the gbeta1 domain by computational design and by in vitro evolution: structural and energetic basis of stabilization. Wunderlich, M., Max, K.E., Roske, Y. et al. J Mol Biol (2007) 373:775-784. DOI 10.1016/j.jmb.2007.08.004 · PubMed
Other PDB entries of the same protein (UniProt P19909 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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