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Cryo-EM structure of heparin-induced 2N4R tau twister filaments

Analyse Cryo-EM structure of heparin-induced 2N4R tau twister filaments in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6QJM
Type: protein
Length: 111 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 1 · best druggability 0.50

Structure

electron microscopy · 1 distinct chain · 0% helix, 59% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Microtubule-associated protein tau	protein	37	0% helix, 59% strand	P10636

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	165	0.50	0.78	21	empty

Interfaces

3 interfaces between chains.

A–C · 1732 Å² buried · 55 hydrogen bonds · protein-protein
A–B · 1729 Å² buried · 55 hydrogen bonds · protein-protein
B–C · 149 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6QJM · Cryo-EM structure of heparin-induced 2N4R tau twister filaments · 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 6QJM · PDBe 6QJM · UniProt P10636

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