MolNFT v1 · #184894 · protein

Argyrophilic grain disease type 1 tau filament

7P6D · Microtubule-associated protein tau: “Argyrophilic grain disease type 1 tau filament”. Electron microscopy, 8 pockets (best druggability 0.74). MolNFT v1 #184894 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7P6D
Type: protein
Length: 575 residues
Chains: 5
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 8 · best druggability 0.74

Structure

electron microscopy · 1 distinct chain · 0% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E	Microtubule-associated protein tau	protein	115	0% helix, 55% strand	P10636

Pockets

8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	554	0.74	0.82	55	empty
2	223	0.72	0.87	37	empty
3	543	0.61	0.74	37	empty
4	51	0.59	0.92	30	empty
5	386	0.59	0.76	30	empty

Interfaces

7 interfaces between chains.

B–C · 4827 Å² buried · 136 hydrogen bonds · protein-protein
D–E · 4825 Å² buried · 135 hydrogen bonds · protein-protein
A–E · 4823 Å² buried · 134 hydrogen bonds · protein-protein
A–C · 4822 Å² buried · 135 hydrogen bonds · protein-protein
A–D · 30 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7P6D · Argyrophilic grain disease type 1 tau filament · 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 7P6D · PDBe 7P6D · UniProt P10636

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