Backbone Modifications in the Protein GB1 Loops: beta-3-Val21, beta-3-Asp40. Determined by X-ray diffraction at 1.95 Å resolution. Released 4 Sept 2013.
Explore 4KGS in 3D Show helices and sheets RCSB PDB PDBe
4KGS contains 3 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 | 2-8 | 7 | 1 |
| β-strand | 13-19 | 7 | 1 |
| α-helix | 23-36 | 14 | |
| β-strand | 42-46 | 5 | 1 |
| α-helix | 47-49 | 3 | |
| β-strand | 51-55 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-8 | 7 | 2 |
| β-strand | 12-19 | 8 | 2 |
| α-helix | 23-36 | 14 | |
| β-strand | 42-46 | 5 | 2 |
| β-strand | 51-55 | 5 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Streptococcal Protein GB1 Backbone Modified Variant: beta-3-Val21, beta-3-Asp40 | A, B | protein | 57 | P06654 (AlphaFold model) |
>4KGS_1 Streptococcal Protein GB1 Backbone Modified Variant: beta-3-Val21, beta-3-Asp40 (chains A, B) DTYKLILNGKTLKGETTTEAXDAATAEKVFKQYANDNGVDGEWTYDDATKTFTVTEX
Protein-like Tertiary Folding Behavior from Heterogeneous Backbones. Reinert, Z.E., Lengyel, G.A., Horne, W.S. J Am Chem Soc (2013) 135:12528-12531. DOI 10.1021/ja405422v · PubMed
Other PDB entries of the same protein (UniProt P06654 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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