3SGP: Alpha-crystallin B chain

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.

Method
X-ray diffraction
Resolution
1.4 Å
Organism
Homo sapiens
Chains
4
Atoms
457
Mol. weight
5.21 kDa
Ligands
MRD
Released
21 Mar 2012

Explore 3SGP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chains A, B, C and D: 0 helices, 1 β-strand

ElementResiduesLengthSheet
β-strand2-1091

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-crystallin B chainA, B, C, Dprotein11Homo sapiensP02511 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>3SGP_1 Alpha-crystallin B chain (chains A, B, C, D)
KLKVLGDVIEV

Ligands and cofactors

IDNameFormulaCopies
MRD(4R)-2-methylpentane-2,4-diolC6 H14 O21

Water and common crystallization additives (MPD) are not listed.

Primary citation

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:

Browse structure collections

About this viewer

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