MolNFT v2 · #215991 · protein

Lipidic amyloid-beta(1-40) fibril - polymorph L2-L3

8OWE · Amyloid-beta A4 protein: “Lipidic amyloid-beta(1-40) fibril - polymorph L2-L3”. Electron microscopy at 3.75, 1 pocket (best druggability 0.30). MolNFT v2 #215991 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 8OWE
Type: protein
Length: 385 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 3.75
Source: Homo sapiens
Molecule: Amyloid-beta A4 protein
UniProt: B4DM00
Pockets: 1 · best druggability 0.30

Structure

electron microscopy · resolution 3.75 · 2 distinct chains · 0% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Amyloid-beta A4 protein	protein	37	0% helix, 35% strand	B4DM00
F, G, H, I, J	Amyloid-beta A4 protein	protein	40	0% helix, 78% strand	B4DM00

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	70	0.30	0.73	19	empty

Interfaces

23 interfaces between chains.

G–H · 1710 Å² buried · 59 hydrogen bonds · protein-protein
F–G · 1708 Å² buried · 59 hydrogen bonds · protein-protein
H–I · 1705 Å² buried · 59 hydrogen bonds · protein-protein
I–J · 1697 Å² buried · 59 hydrogen bonds · protein-protein
C–D · 1635 Å² buried · 44 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 8OWE · PDBe 8OWE · UniProt B4DM00

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