MolNFT v1 · #161608 · protein

Cryo-EM structure of heparin-induced 2N3R tau filaments

6QJQ · Microtubule-associated protein tau: “Cryo-EM structure of heparin-induced 2N3R tau filaments”. Electron microscopy, 2 pockets (best druggability 0.54). MolNFT v1 #161608 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6QJQ
Type: protein
Length: 162 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 0.54

Structure

electron microscopy · 2 distinct chains · 0% helix, 59% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Microtubule-associated protein tau	protein	28	0% helix, 54% strand	P10636
D, E, F	Microtubule-associated protein tau	protein	26	0% helix, 65% 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	89	0.54	0.83	12	empty
2	265	0.48	0.73	41	empty

Interfaces

11 interfaces between chains.

A–C · 1222 Å² buried · 31 hydrogen bonds · protein-protein
D–F · 1174 Å² buried · 34 hydrogen bonds · protein-protein
A–B · 1146 Å² buried · 27 hydrogen bonds · protein-protein
D–E · 1105 Å² buried · 27 hydrogen bonds · protein-protein
C–F · 461 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

6QJQ · Cryo-EM structure of heparin-induced 2N3R tau 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 6QJQ · PDBe 6QJQ · UniProt P10636

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