NMR Structure of Human apoS100B at 10C. Determined by solution NMR. Released 15 Apr 2008.
Explore 2PRU in 3D Show helices and sheets RCSB PDB PDBe
2PRU contains 8 α-helices and 4 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 |
|---|---|---|---|
| α-helix | 2-16 | 15 | |
| β-strand | 27 | 1 | 1 |
| α-helix | 29-38 | 10 | |
| α-helix | 49-63 | 15 | |
| β-strand | 68 | 1 | 1 |
| α-helix | 70-81 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein S100-B | A, B | protein | 91 | Homo sapiens | P04271 (AlphaFold model) |
>2PRU_1 Protein S100-B (chains A, B) SELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETL DNDGDGECDFQEFMAFVAMVTTACHEFFEHE
Analysis of the structure of human apo-S100B at low temperature indicates a unimodal conformational distribution is adopted by calcium-free S100 proteins. Malik, S., Revington, M., Smith, S.P. et al. Proteins (2008) 73:28-42. DOI 10.1002/prot.22037 · PubMed
Other PDB entries of the same protein (UniProt P04271 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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