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Straight filament from sporadic ALZHEIMER'S disease brain

Analyse Straight filament from sporadic ALZHEIMER'S disease brain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6HRF
Type: protein
Length: 462 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 0.35

Structure

electron microscopy · 1 distinct chain · 0% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Microtubule-associated protein tau	protein	77	0% helix, 45% strand	P10636

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.35	0.77	15	empty
2	57	0.33	0.77	19	empty

Interfaces

9 interfaces between chains.

C–E · 3257 Å² buried · 85 hydrogen bonds · protein-protein
A–C · 3254 Å² buried · 85 hydrogen bonds · protein-protein
D–F · 3227 Å² buried · 78 hydrogen bonds · protein-protein
B–D · 3216 Å² buried · 71 hydrogen bonds · protein-protein
E–F · 107 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

6HRF · Straight filament from sporadic Alzheimer's disease brain · 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 6HRF · PDBe 6HRF · UniProt P10636

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