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Straight filament from ALZHEIMER'S disease with pet ligand apn-1607

Analyse Straight filament from ALZHEIMER'S disease with pet ligand apn-1607 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7NRX
Type: protein
Length: 770 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 4 · best druggability 0.63

Structure

electron microscopy · 1 distinct chain · 0% helix, 42% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, I, B, C, D, E, F, G, H, J	Microtubule-associated protein tau	protein	77	0% helix, 42% strand	P10636

Pockets

4 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	374	0.63	0.78	35	empty
2	282	0.62	0.80	30	empty
3	55	0.42	0.82	21	empty
4	60	0.26	0.72	12	empty

Interfaces

20 interfaces between chains.

B–D · 3283 Å² buried · 95 hydrogen bonds · protein-protein
A–B · 3281 Å² buried · 95 hydrogen bonds · protein-protein
A–F · 3278 Å² buried · 94 hydrogen bonds · protein-protein
F–H · 3270 Å² buried · 93 hydrogen bonds · protein-protein
G–J · 3264 Å² buried · 95 hydrogen bonds · protein-protein

Compared structures

7NRX · Straight filament from Alzheimer's disease with PET ligand APN-1607 · the same entry in another collection · chain A against A, 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 P10636
Elsewhere: RCSB PDB 7NRX · PDBe 7NRX · UniProt P10636

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