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Straight tau filaments in dominantly inherited Alzheimer disease with cotton wool plaques

Analyse Straight tau filaments in dominantly inherited Alzheimer disease with cotton… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 9CZL
Type: protein
Length: 740 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.9
Source: Homo sapiens
Molecule: Isoform Tau-C of Microtubule-associated protein tau
UniProt: P10636
Pockets: 4 · best druggability 0.63

Structure

electron microscopy · resolution 2.9 · 1 distinct chain · 0% helix, 70% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J	Isoform Tau-C of Microtubule-associated protein tau	protein	74	0% helix, 70% strand	P10636

Pockets

4 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	504	0.63	0.76	47	empty
2	212	0.55	0.79	33	empty
3	89	0.35	0.75	22	empty
4	63	0.33	0.76	20	empty

Interfaces

20 interfaces between chains.

G–I · 3104 Å² buried · 82 hydrogen bonds · protein-protein
E–G · 3100 Å² buried · 82 hydrogen bonds · protein-protein
C–E · 3099 Å² buried · 82 hydrogen bonds · protein-protein
A–C · 3095 Å² buried · 82 hydrogen bonds · protein-protein
D–F · 3086 Å² buried · 84 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 9CZL · PDBe 9CZL · UniProt P10636

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