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Abeta fibril (morphology I)

Analyse Abeta fibril (morphology I) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SHS
Type: protein
Length: 480 residues
Chains: 12
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amyloid-beta precursor protein
UniProt: P05067
Pockets: 9 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 0% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, H, D, I, E, J, F, K, G, L	Amyloid-beta precursor protein	protein	40	0% helix, 45% strand	P05067

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	638	0.78	0.83	84	empty
2	535	0.75	0.83	63	empty
3	176	0.71	0.89	49	empty
4	111	0.69	0.91	34	empty
5	173	0.68	0.87	51	empty

Interfaces

30 interfaces between chains.

J–K · 1690 Å² buried · 46 hydrogen bonds · protein-protein
H–I · 1686 Å² buried · 46 hydrogen bonds · protein-protein
C–D · 1686 Å² buried · 45 hydrogen bonds · protein-protein
B–J · 1684 Å² buried · 46 hydrogen bonds · protein-protein
K–L · 1683 Å² buried · 46 hydrogen bonds · protein-protein

Compared structures

6SHS · Abeta fibril (Morphology I) · the same entry in another collection · chain L against L, TM-score 1.00

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 6SHS · PDBe 6SHS · UniProt P05067

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