Amyloid-related segment of alphaB-crystallin residues 90-100 mutant V91L. Determined by X-ray diffraction at 1.4 Å resolution. Released 21 Mar 2012.
Explore 3SGP in 3D Show helices and sheets RCSB PDB PDBe
3SGP contains 0 α-helices and 4 β-strands across 4 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 |
|---|---|---|---|
| β-strand | 2-10 | 9 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Alpha-crystallin B chain | A, B, C, D | protein | 11 | Homo sapiens | P02511 (AlphaFold model) |
>3SGP_1 Alpha-crystallin B chain (chains A, B, C, D) KLKVLGDVIEV
| ID | Name | Formula | Copies |
|---|---|---|---|
| MRD | (4R)-2-methylpentane-2,4-diol | C6 H14 O2 | 1 |
Water and common crystallization additives (MPD) are not listed.
Atomic view of a toxic amyloid small oligomer. Laganowsky, A., Liu, C., Sawaya, M.R. et al. Science (2012) 335:1228-1231. DOI 10.1126/science.1213151 · PubMed
Other PDB entries of the same protein (UniProt P02511 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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