1SYM: S100B

3-D solution structure of reduced apo-S100B from rat, NMR, 20 structures. Determined by solution NMR. Released 7 Dec 1996.

Method
Solution NMR
Organism
Rattus norvegicus
Chains
2
Atoms
1,502
Mol. weight
21.52 kDa
Released
7 Dec 1996

Explore 1SYM in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A and B: 8 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix2-32
α-helix4-85
α-helix9-135
α-helix14-185
β-strand27-2821
α-helix29-346
α-helix35-406
α-helix50-6314
β-strand67-6821
α-helix70-8112

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
S100BA, Bprotein92Rattus norvegicusP04631 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>1SYM_1 S100B (chains A, B)
MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMET
LDEDGDGECDFQEFMAFVSMVTTACHEFFEHE

Primary citation

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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