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High-resolution MAP of tau filament from progressive supranuclear palsy (psp) case 1

Analyse High-resolution MAP of tau filament from progressive supranuclear palsy (psp)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7U0Z
Type: protein
Length: 330 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Isoform tau-E of microtubule-associated protein tau
UniProt: P10636
Pockets: 6 · best druggability 0.53

Structure

electron microscopy · 1 distinct chain · 0% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, C, A	Isoform tau-E of microtubule-associated protein tau	protein	110	0% helix, 52% strand	P10636

Pockets

6 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	152	0.53	0.79	18	empty
2	108	0.51	0.81	19	empty
3	104	0.46	0.79	17	empty
4	142	0.38	0.73	22	empty
5	60	0.37	0.80	15	empty

Interfaces

3 interfaces between chains.

B–C · 4614 Å² buried · 125 hydrogen bonds · protein-protein
B–A · 4604 Å² buried · 125 hydrogen bonds · protein-protein
C–A · 145 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7U0Z · High-resolution map of tau filament from progressive supranuclear palsy (PSP) case 1 · the same entry in another collection · chain B against B, 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 7U0Z · PDBe 7U0Z · UniProt P10636

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