Solution structure of rat apo-S100B using dipolar couplings. Determined by solution NMR. Released 30 Dec 1998.
Explore 1B4C in 3D Show helices and sheets RCSB PDB PDBe
1B4C contains 10 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 | 2-17 | 16 | |
| β-strand | 27 | 1 | 1 |
| α-helix | 29-39 | 11 | |
| α-helix | 43-46 | 4 | |
| α-helix | 50-61 | 12 | |
| β-strand | 68 | 1 | 1 |
| α-helix | 70-83 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein (S-100 protein, beta chain) | A, B | protein | 92 | Rattus norvegicus | P04631 (AlphaFold model) |
>1B4C_1 PROTEIN (S-100 PROTEIN, BETA CHAIN) (chains A, B) MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMET LDEDGDGECDFQEFMAFVSMVTTACHEFFEHE
The use of dipolar couplings for determining the solution structure of rat apo-S100B(betabeta). Drohat, A.C., Tjandra, N., Baldisseri, D.M. et al. Protein Sci (1999) 8:800-809. 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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