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Globular glial tauopathy type 3 tau filament

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

PDB: 7P68
Type: protein
Length: 1,080 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 10 · best druggability 0.73

Structure

electron microscopy · 1 distinct chain · 0% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, E, G, I, D, F, H, J	Microtubule-associated protein tau	protein	108	0% helix, 55% strand	P10636

Pockets

10 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1029	0.73	0.76	78	empty
2	186	0.72	0.89	30	empty
3	145	0.70	0.90	30	empty
4	171	0.69	0.87	34	empty
5	107	0.64	0.88	34	empty

Interfaces

27 interfaces between chains.

A–I · 4573 Å² buried · 154 hydrogen bonds · protein-protein
A–E · 4566 Å² buried · 152 hydrogen bonds · protein-protein
B–D · 4563 Å² buried · 150 hydrogen bonds · protein-protein
B–H · 4558 Å² buried · 149 hydrogen bonds · protein-protein
H–J · 4557 Å² buried · 150 hydrogen bonds · protein-protein

Compared structures

7P68 · Globular glial tauopathy type 3 tau filament · the same entry in another collection · chain D against D, 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 7P68 · PDBe 7P68 · UniProt P10636

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