Structure of Streptococcal protein G B1 domain at pH 3.0. Determined by X-ray diffraction at 1.2 Å resolution. Released 23 Feb 2011.
Explore 3MP9 in 3D Show helices and sheets RCSB PDB PDBe
3MP9 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 | 9-16 | 8 | 1 |
| β-strand | 21-28 | 8 | 1 |
| α-helix | 31-44 | 14 | |
| β-strand | 50-54 | 5 | 1 |
| β-strand | 59-63 | 5 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Immunoglobulin G-binding protein G | A, B | protein | 64 | Streptococcus sp. 'group G' | P06654 (AlphaFold model) |
>3MP9_1 Immunoglobulin G-binding protein G (chains A, B) HHHHHHAMDTYKLILNGKTLKGETTTEAVDAATAEKVFKQYANDNGVDGEWTYDDATKTF TVTE
Structural origins of pH-dependent chemical shifts in the B1 domain of protein G. Tomlinson, J.H., Green, V.L., Baker, P.J. et al. Proteins (2010) 78:3000-3016. DOI 10.1002/prot.22825 · 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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