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Limbic-predominant neuronal inclusion body 4R tauopathy type 1A tau filament

Analyse Limbic-predominant neuronal inclusion body 4R tauopathy type 1A tau filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7P6A
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: 2 · best druggability 0.73

Structure

electron microscopy · 1 distinct chain · 0% helix, 63% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Microtubule-associated protein tau	protein	108	0% helix, 63% strand	P10636

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	887	0.73	0.78	72	empty
2	83	0.32	0.73	18	empty

Interfaces

7 interfaces between chains.

D–E · 4509 Å² buried · 155 hydrogen bonds · protein-protein
A–D · 4509 Å² buried · 155 hydrogen bonds · protein-protein
B–C · 4508 Å² buried · 158 hydrogen bonds · protein-protein
A–B · 4506 Å² buried · 155 hydrogen bonds · protein-protein
B–D · 73 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7P6A · Limbic-predominant neuronal inclusion body 4R tauopathy type 1a 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 7P6A · PDBe 7P6A · UniProt P10636

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