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Lipidic amyloid-beta(1-40) fibril - polymorph L1

Analyse Lipidic amyloid-beta(1-40) fibril - polymorph L1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8OVK
Type: protein
Length: 400 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.88
Source: Homo sapiens
Molecule: Amyloid-beta A4 protein
UniProt: B4DM00
Pockets: 1 · best druggability 0.70

Structure

electron microscopy · resolution 2.88 · 1 distinct chain · 0% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J	Amyloid-beta A4 protein	protein	40	0% helix, 58% strand	B4DM00

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	172	0.70	0.89	40	empty

Interfaces

23 interfaces between chains.

E–G · 1672 Å² buried · 57 hydrogen bonds · protein-protein
G–I · 1670 Å² buried · 57 hydrogen bonds · protein-protein
C–E · 1669 Å² buried · 57 hydrogen bonds · protein-protein
F–H · 1668 Å² buried · 57 hydrogen bonds · protein-protein
A–C · 1668 Å² buried · 57 hydrogen bonds · protein-protein

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 B4DM00
Elsewhere: RCSB PDB 8OVK · PDBe 8OVK · UniProt B4DM00

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