Research workbench

A new structural model of ABETA(1-40) fibrils

Analyse A new structural model of ABETA(1-40) fibrils in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6TI5
Type: protein
Length: 480 residues
Chains: 16
Method: solid-state nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Amyloid-beta precursor protein
UniProt: P05067
Pockets: 5 · best druggability 0.79

Structure

solid-state nmr · 1 distinct chain · 0% helix, 70% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P	Amyloid-beta precursor protein	protein	30	0% helix, 70% strand	P05067

Pockets

5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	361	0.79	0.89	68	empty
2	382	0.78	0.88	72	empty
3	110	0.73	0.94	48	empty
4	498	0.61	0.75	42	empty
5	437	0.59	0.74	40	empty

Interfaces

48 interfaces between chains.

K–L · 1414 Å² buried · 45 hydrogen bonds · protein-protein
F–G · 1408 Å² buried · 44 hydrogen bonds · protein-protein
C–D · 1407 Å² buried · 43 hydrogen bonds · protein-protein
N–O · 1404 Å² buried · 42 hydrogen bonds · protein-protein
M–N · 1403 Å² buried · 41 hydrogen bonds · protein-protein

Compared structures

6TI5 · A New Structural Model of Abeta(1-40) Fibrils · the same entry in another collection · chain K against K, 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 6TI5 · PDBe 6TI5 · UniProt P05067

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.