solution structure of PSD-1. Determined by solution NMR. Released 5 Dec 2006.
Explore 2FS1 in 3D Show helices and sheets RCSB PDB PDBe
2FS1 contains 3 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 5-23 | 19 | |
| α-helix | 27-34 | 8 | |
| α-helix | 40-51 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| PSD-1 | A | protein | 56 | Finegoldia magna ATCC 29328, Streptococcus dysgalactiae, Streptococcus equi, Streptococcus canis, Streptococcus sp. | Q51918 (AlphaFold model) |
>2FS1_1 PSD-1 (chains A) MEAVDANSLAQAKEAAIKELKQYGIGDYYIKLINNAKTVEGVESLKNEILKALPTE
Structure, dynamics, and stability variation in bacterial albumin binding modules: implications for species specificity. He, Y., Rozak, D.A., Sari, N. et al. Biochemistry (2006) 45:10102-10109. DOI 10.1021/bi060409m · PubMed
Other PDB entries of the same protein (UniProt Q51918 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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