MolNFT v1 · #128881 · protein

Straight filament in ALZHEIMER'S disease brain

5O3T · Microtubule-associated protein tau: “Straight filament in ALZHEIMER'S disease brain”. Electron microscopy, 5 pockets (best druggability 0.68). MolNFT v1 #128881 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5O3T
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: 5 · best druggability 0.68

Structure

electron microscopy · 1 distinct chain · 0% helix, 25% 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, 25% strand	P10636

Pockets

5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	164	0.68	0.87	33	empty
2	140	0.67	0.88	30	empty
3	337	0.58	0.76	29	empty
4	50	0.56	0.91	25	empty
5	197	0.51	0.77	38	empty

Interfaces

27 interfaces between chains.

C–E · 3174 Å² buried · 88 hydrogen bonds · protein-protein
E–G · 3171 Å² buried · 88 hydrogen bonds · protein-protein
A–C · 3169 Å² buried · 88 hydrogen bonds · protein-protein
H–J · 3169 Å² buried · 86 hydrogen bonds · protein-protein
F–H · 3168 Å² buried · 87 hydrogen bonds · protein-protein

Compared structures

5O3T · Straight 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 5O3T · PDBe 5O3T · UniProt P10636

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.