Research workbench

Chronic traumatic encephalopathy type II tau filament

Analyse Chronic traumatic encephalopathy type II tau filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6NWQ
Type: protein
Length: 450 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 2 · best druggability 0.53

Structure

electron microscopy · 1 distinct chain · 0% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Microtubule-associated protein tau	protein	75	0% helix, 35% strand	P10636

Pockets

2 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	151	0.53	0.79	24	empty
2	145	0.51	0.79	24	empty

Interfaces

11 interfaces between chains.

A–C · 3137 Å² buried · 81 hydrogen bonds · protein-protein
A–E · 3130 Å² buried · 80 hydrogen bonds · protein-protein
B–F · 3127 Å² buried · 83 hydrogen bonds · protein-protein
B–D · 3125 Å² buried · 79 hydrogen bonds · protein-protein
E–F · 282 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

6NWQ · Chronic traumatic encephalopathy Type II 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 6NWQ · PDBe 6NWQ · UniProt P10636

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