3-D solution structure of reduced apo-S100B from rat, NMR, 20 structures. Determined by solution NMR. Released 7 Dec 1996.
Explore 1SYM in 3D Show helices and sheets RCSB PDB PDBe
1SYM contains 16 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 | 2-3 | 2 | |
| α-helix | 4-8 | 5 | |
| α-helix | 9-13 | 5 | |
| α-helix | 14-18 | 5 | |
| β-strand | 27-28 | 2 | 1 |
| α-helix | 29-34 | 6 | |
| α-helix | 35-40 | 6 | |
| α-helix | 50-63 | 14 | |
| β-strand | 67-68 | 2 | 1 |
| α-helix | 70-81 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| S100B | A, B | protein | 92 | Rattus norvegicus | P04631 (AlphaFold model) |
>1SYM_1 S100B (chains A, B) MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMET LDEDGDGECDFQEFMAFVSMVTTACHEFFEHE
Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy. Drohat, A.C., Amburgey, J.C., Abildgaard, F. et al. Biochemistry (1996) 35:11577-11588. DOI 10.1021/bi9612226 · PubMed
Other PDB entries of the same protein (UniProt P04631 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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