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Globular glial tauopathy type 1 tau filament

Analyse Globular glial tauopathy type 1 tau filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7P66
Type: protein
Length: 540 residues
Chains: 5
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 5 · best druggability 0.75

Structure

electron microscopy · 1 distinct chain · 0% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Microtubule-associated protein tau	protein	108	0% helix, 56% strand	P10636

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	984	0.75	0.78	77	empty
2	183	0.72	0.89	28	empty
3	92	0.62	0.88	33	empty
4	155	0.39	0.73	20	empty
5	73	0.29	0.73	15	empty

Interfaces

7 interfaces between chains.

A–D · 4601 Å² buried · 147 hydrogen bonds · protein-protein
B–C · 4598 Å² buried · 146 hydrogen bonds · protein-protein
A–B · 4597 Å² buried · 147 hydrogen bonds · protein-protein
D–E · 4593 Å² buried · 146 hydrogen bonds · protein-protein
A–E · 135 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7P66 · Globular glial tauopathy type 1 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 7P66 · PDBe 7P66 · UniProt P10636

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