Research workbench

In vitro assembled 266/297 - 391 tau filaments with ZNCL2 (11A)

Analyse In vitro assembled 266/297 - 391 tau filaments with ZNCL2 (11A) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QKL
Type: protein
Length: 456 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 0.59

Structure

electron microscopy · 1 distinct chain · 0% helix, 68% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Microtubule-associated protein tau	protein	76	0% helix, 68% 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	288	0.59	0.78	33	empty
2	272	0.57	0.77	33	empty
3	128	0.36	0.73	22	empty
4	71	0.28	0.72	17	empty

Interfaces

8 interfaces between chains.

A–C · 3198 Å² buried · 93 hydrogen bonds · protein-protein
E–F · 3189 Å² buried · 93 hydrogen bonds · protein-protein
D–F · 3186 Å² buried · 91 hydrogen bonds · protein-protein
B–C · 3169 Å² buried · 92 hydrogen bonds · protein-protein
B–D · 160 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7QKL · In vitro assembled 266/297 - 391 tau filaments with ZnCl2 (11a) · 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 7QKL · PDBe 7QKL · UniProt P10636

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.