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Argyrophilic grain disease type 2 tau filament

Analyse Argyrophilic grain disease type 2 tau filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7P6E
Type: protein
Length: 1,050 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 13 · best druggability 0.76

Structure

electron microscopy · 1 distinct chain · 0% helix, 34% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, I, J, Q, R	Microtubule-associated protein tau	protein	105	0% helix, 34% strand	P10636

Pockets

13 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	422	0.76	0.85	57	empty
2	431	0.75	0.84	56	empty
3	269	0.71	0.86	34	empty
4	149	0.69	0.89	34	empty
5	261	0.66	0.83	35	empty

Interfaces

21 interfaces between chains.

A–C · 4435 Å² buried · 124 hydrogen bonds · protein-protein
A–E · 4429 Å² buried · 122 hydrogen bonds · protein-protein
B–D · 4424 Å² buried · 122 hydrogen bonds · protein-protein
B–F · 4424 Å² buried · 124 hydrogen bonds · protein-protein
D–R · 4371 Å² buried · 118 hydrogen bonds · protein-protein

Compared structures

7P6E · Argyrophilic grain disease type 2 tau filament · 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 7P6E · PDBe 7P6E · UniProt P10636

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