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Paired helical filament from primary age-related tauopathy brain

Analyse Paired helical filament from primary age-related tauopathy brain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7NRQ
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 0.37

Structure

electron microscopy · 1 distinct chain · 0% helix, 48% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J	Microtubule-associated protein tau	protein	77	0% helix, 48% strand	P10636

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.37	0.74	19	empty
2	80	0.34	0.75	19	empty
3	86	0.33	0.74	16	empty
4	76	0.28	0.72	12	empty

Interfaces

20 interfaces between chains.

H–J · 3236 Å² buried · 101 hydrogen bonds · protein-protein
C–E · 3216 Å² buried · 102 hydrogen bonds · protein-protein
A–G · 3205 Å² buried · 91 hydrogen bonds · protein-protein
B–H · 3204 Å² buried · 89 hydrogen bonds · protein-protein
D–F · 3201 Å² buried · 93 hydrogen bonds · protein-protein

Compared structures

7NRQ · Paired helical filament from primary age-related tauopathy brain · 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 7NRQ · PDBe 7NRQ · UniProt P10636

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