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In vitro assembled 266/297 - 391 tau filaments with licl (9A)

Analyse In vitro assembled 266/297 - 391 tau filaments with licl (9A) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QJY
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, 61% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Microtubule-associated protein tau	protein	75	0% helix, 61% 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	154	0.53	0.79	26	empty
2	131	0.52	0.80	24	empty

Interfaces

12 interfaces between chains.

C–F · 3190 Å² buried · 89 hydrogen bonds · protein-protein
B–D · 3174 Å² buried · 88 hydrogen bonds · protein-protein
C–E · 3158 Å² buried · 87 hydrogen bonds · protein-protein
A–D · 3144 Å² buried · 88 hydrogen bonds · protein-protein
D–E · 88 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7QJY · In vitro assembled 266/297 - 391 tau filaments with LiCl (9a) · 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 7QJY · PDBe 7QJY · UniProt P10636

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