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UniProt B4DM00

Amyloid-beta A4 protein (B4DM00)

Amyloid-beta A4 protein (UniProt B4DM00): 8 experimental structures on GenesisL1, 2 ligands bound, 6 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
B4DM00
Protein
Amyloid-beta A4 protein
Experimental structures
8
Predicted models
0
Ligands
2
Pockets
6 · 3 records with a druggable one

Structures

8 records of B4DM00 in the MolNFT archive: 8 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
7F29Cryo-EM structure of the fibril formed by disaccharide-modified amyloid-BETA(1-42)electron microscopyE, C, D, F, A, BX6X—
8B9QMolecular structure of Cu(II)-bound amyloid-beta monomer implicated in inhibition of peptide…solution nmrACU—
8B9RMolecular structure of Cu(II)-bound amyloid-beta monomer implicated in inhibition of peptide…solution nmrACU—
8OT1unseeded Abeta(1-40) amyloid fibril (morphology i)electron microscopyA, B, C, D, E, F, G, H, I, J, K, L—1 (best 0.78)
8OT3unseeded Abeta(1-40) amyloid fibril (morphology ii)electron microscopyA, B, C, D, E, F, G, H, I, J, K, L—3 (best 0.76)
8OVKLipidic amyloid-beta(1-40) fibril - polymorph L1electron microscopyA, B, C, D, E, F, G, H, I, J—1 (best 0.70)
8OWELipidic amyloid-beta(1-40) fibril - polymorph L2-L3electron microscopyA, B, C, D, E, F, G, H, I, J—1 (best 0.30)
8OWJLipidic amyloid-beta(1-40) fibril - polymorph L2-L2electron microscopyE, A, B, C, D, F, G, H, I, J——

Ligands

  • CU · Copper (II) ion · in 2 records
  • X6X · 2-amino-2-deoxy-alpha-D-galactopyranose · in 1 record

Elsewhere

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