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Tau - CTE-MIA4 (tau intermediate amyloid)

Analyse Tau - CTE-MIA4 (tau intermediate amyloid) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8Q8W
Type: protein
Length: 429 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.85
Source: Homo sapiens
Molecule: Isoform Tau-D of Microtubule-associated protein tau
UniProt: P10636
Pockets: 5 · best druggability 0.52

Structure

electron microscopy · resolution 2.85 · 2 distinct chains · 0% helix, 65% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, A, E	Isoform Tau-D of Microtubule-associated protein tau	protein	68	0% helix, 63% strand	P10636
B, D, F	Isoform Tau-D of Microtubule-associated protein tau	protein	75	0% helix, 67% strand	P10636

Pockets

5 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	123	0.52	0.80	22	empty
2	143	0.52	0.79	25	empty
3	50	0.40	0.83	17	empty
4	64	0.28	0.73	19	empty
5	72	0.27	0.72	14	empty

Interfaces

9 interfaces between chains.

B–F · 3141 Å² buried · 85 hydrogen bonds · protein-protein
B–D · 3123 Å² buried · 88 hydrogen bonds · protein-protein
A–E · 2858 Å² buried · 80 hydrogen bonds · protein-protein
C–E · 2843 Å² buried · 74 hydrogen bonds · protein-protein
A–D · 233 Å² buried · 5 hydrogen bonds · protein-protein

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 8Q8W · PDBe 8Q8W · UniProt P10636

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