Research workbench

In vitro assembled 266/297 - 391 tau filaments with MGSO4 and nacl (15C)

Analyse In vitro assembled 266/297 - 391 tau filaments with MGSO4 and nacl (15C) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QL0
Type: protein
Length: 414 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 3 · best druggability 0.52

Structure

electron microscopy · 1 distinct chain · 0% helix, 55% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, c, A, C, D, E	Microtubule-associated protein tau	protein	69	0% helix, 55% strand	P10636

Pockets

3 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	129	0.52	0.80	22	empty
2	132	0.52	0.79	23	empty
3	144	0.46	0.77	19	empty

Interfaces

12 interfaces between chains.

C–D · 2856 Å² buried · 79 hydrogen bonds · protein-protein
B–A · 2843 Å² buried · 77 hydrogen bonds · protein-protein
B–c · 2842 Å² buried · 85 hydrogen bonds · protein-protein
C–E · 2840 Å² buried · 75 hydrogen bonds · protein-protein
A–C · 155 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

7QL0 · In vitro assembled 266/297 - 391 tau filaments with MgSO4 and NaCl (15c) · 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 7QL0 · PDBe 7QL0 · UniProt P10636

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