MolNFT v1 · #128873 · protein

Paired helical filament in ALZHEIMER'S disease brain

5O3L · Microtubule-associated protein tau: “Paired helical filament in ALZHEIMER'S disease brain”. Electron microscopy, 4 pockets (best druggability 0.45). MolNFT v1 #128873 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5O3L
Type: protein
Length: 730 residues
Chains: 10
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 4 · best druggability 0.45

Structure

electron microscopy · 1 distinct chain · 0% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, H, I, J	Microtubule-associated protein tau	protein	73	0% helix, 29% strand	P10636

Pockets

4 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	143	0.45	0.77	23	empty
2	114	0.44	0.78	29	empty
3	131	0.43	0.76	21	empty
4	105	0.42	0.78	26	empty

Interfaces

24 interfaces between chains.

C–E · 3113 Å² buried · 94 hydrogen bonds · protein-protein
H–J · 3112 Å² buried · 93 hydrogen bonds · protein-protein
E–G · 3112 Å² buried · 94 hydrogen bonds · protein-protein
G–I · 3111 Å² buried · 94 hydrogen bonds · protein-protein
F–H · 3109 Å² buried · 93 hydrogen bonds · protein-protein

Compared structures

5O3L · Paired helical filament in 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 5O3L · PDBe 5O3L · UniProt P10636

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