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3D structure of ALZHEIMER'S ABETA(1-42) fibrils

Analyse 3D structure of ALZHEIMER'S ABETA(1-42) fibrils in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2BEG
Type: protein
Length: 130 residues
Chains: 5
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amyloid beta A4 protein
UniProt: P05067
Pockets: 2 · best druggability 0.52

Structure

solution nmr · 1 distinct chain · 0% helix, 77% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Amyloid beta A4 protein	protein	26	0% helix, 77% strand	P05067

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	95	0.52	0.83	25	empty
2	65	0.51	0.85	25	empty

Interfaces

7 interfaces between chains.

A–B · 1203 Å² buried · 42 hydrogen bonds · protein-protein
B–C · 1140 Å² buried · 40 hydrogen bonds · protein-protein
D–E · 1136 Å² buried · 38 hydrogen bonds · protein-protein
C–D · 1110 Å² buried · 38 hydrogen bonds · protein-protein
A–C · 122 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2BEG · 3D Structure of Alzheimer's Abeta(1-42) fibrils · the same entry in another collection · chain E against E, TM-score 1.00
P05067 · AlphaFold monomer V2.0 prediction for amyloid-beta precursor protein (P05067) · a predicted model of the same protein · chain A against A, TM-score 0.31

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P05067
Elsewhere: RCSB PDB 2BEG · PDBe 2BEG · UniProt P05067

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