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Progressive supranuclear palsy tau filament

Analyse Progressive supranuclear palsy tau filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7P65
Type: protein
Length: 550 residues
Chains: 5
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 7 · best druggability 0.75

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	110	0% helix, 55% strand	P10636

Pockets

7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	306	0.75	0.87	30	empty
2	307	0.75	0.86	35	empty
3	918	0.75	0.78	68	empty
4	142	0.64	0.87	33	empty
5	61	0.60	0.91	28	empty

Interfaces

9 interfaces between chains.

D–E · 4702 Å² buried · 135 hydrogen bonds · protein-protein
A–D · 4699 Å² buried · 135 hydrogen bonds · protein-protein
A–B · 4697 Å² buried · 135 hydrogen bonds · protein-protein
B–C · 4684 Å² buried · 134 hydrogen bonds · protein-protein
A–E · 162 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

7P65 · Progressive supranuclear palsy 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 7P65 · PDBe 7P65 · UniProt P10636

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