7ROJ: Alpha-crystallin B chain peptide

Amyloid-related segment of alphaB-crystallin residues 90-100 with G95W mutation. Determined by X-ray diffraction at 1.6 Å resolution. Released 12 Jan 2022.

Method
X-ray diffraction
Resolution
1.6 Å
Organism
Homo sapiens
Chains
12
Atoms
1,212
Mol. weight
16.53 kDa
Ligands
TFA
Released
12 Jan 2022

Explore 7ROJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

7ROJ contains 0 α-helices and 12 β-strands across 12 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, D, E, F, G, H, I and J: 0 helices, 1 β-strand

ElementResiduesLengthSheet
β-strand2-1091
Chain K: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand2-982
Chain L: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand3-1082

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-crystallin B chain peptideA, B, C, D, E, F, G, H, I, J, K, Lprotein11Homo sapiensP02511 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F, G, H, I, J, K, L), FASTA
>7ROJ_1 Alpha-crystallin B chain peptide (chains A, B, C, D, E, F, G, H, I, J, K, L)
KVKVLWDVIEV

Ligands and cofactors

IDNameFormulaCopies
TFAtrifluoroacetic acidC2 H F3 O24

Water and common crystallization additives (GOL, NA) are not listed.

Primary citation

Atomic view of an amyloid dodecamer exhibiting selective cellular toxic vulnerability in acute brain slices. Gray, A.L.H., Sawaya, M.R., Acharyya, D. et al. Protein Sci (2022) 31:716-727. DOI 10.1002/pro.4268 · PubMed

Other PDB entries of the same protein (UniProt P02511 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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