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In vitro assembled 297-408 S396D S400D T403D S404D tau filaments (42A)

Analyse In vitro assembled 297-408 S396D S400D T403D S404D tau filaments (42A) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QKI
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: 1 · best druggability 0.35

Structure

electron microscopy · 1 distinct chain · 0% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
D, A, B, C, E, F	Microtubule-associated protein tau	protein	76	0% helix, 58% strand	P10636

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	68	0.35	0.77	17	empty

Interfaces

14 interfaces between chains.

C–E · 3472 Å² buried · 75 hydrogen bonds · protein-protein
C–F · 3341 Å² buried · 75 hydrogen bonds · protein-protein
D–B · 3163 Å² buried · 80 hydrogen bonds · protein-protein
D–A · 3146 Å² buried · 83 hydrogen bonds · protein-protein
E–F · 265 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

7QKI · In vitro assembled 297-408 S396D S400D T403D S404D tau filaments (42a) · the same entry in another collection · chain D against D, 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 7QKI · PDBe 7QKI · UniProt P10636

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