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In vitro assembled 266/297 - 391 tau filaments with nacl (8B)

Analyse In vitro assembled 266/297 - 391 tau filaments with nacl (8B) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QL3
Type: protein
Length: 426 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 4 · best druggability 0.54

Structure

electron microscopy · 1 distinct chain · 0% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Microtubule-associated protein tau	protein	71	0% helix, 51% strand	P10636

Pockets

4 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	139	0.54	0.80	25	empty
2	131	0.53	0.80	24	empty
3	55	0.31	0.76	13	empty
4	54	0.25	0.72	18	empty

Interfaces

10 interfaces between chains.

A–B · 2984 Å² buried · 65 hydrogen bonds · protein-protein
D–F · 2982 Å² buried · 67 hydrogen bonds · protein-protein
D–E · 2969 Å² buried · 63 hydrogen bonds · protein-protein
A–C · 2963 Å² buried · 65 hydrogen bonds · protein-protein
B–D · 178 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7QL3 · in vitro assembled 266/297 - 391 tau filaments with NaCl (8b) · 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 7QL3 · PDBe 7QL3 · UniProt P10636

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