Selenomethionine mutant (A34Sem) of protein GB1 examined by X-ray diffraction. Determined by X-ray diffraction at 1.1 Å resolution. Released 10 Jul 2019.
Explore 6CHE in 3D Show helices and sheets RCSB PDB PDBe
6CHE 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. group G | P19909 (AlphaFold model) |
>6CHE_1 Immunoglobulin G-binding protein G (chains A) GQYKLILNGKTLKGETTTEAVDAATAEKVFKQYMNDNGVDGEWTYDDATKTFTVTE
77Se NMR Probes the Protein Environment of Selenomethionine. Chen, Q., Xu, S., Lu, X. et al. J Phys Chem B (2020) 124:601-616. DOI 10.1021/acs.jpcb.9b07466 · PubMed
Other PDB entries of the same protein (UniProt P19909 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 6CHE directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.