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In vitro assembled tau filaments with MGSO4 and nacl (15A)

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

PDB: 7QKV
Type: protein
Length: 621 residues
Chains: 9
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 7 · best druggability 0.53

Structure

electron microscopy · 1 distinct chain · 0% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A, C, D, E, F, G, H, I	Microtubule-associated protein tau	protein	69	0% helix, 54% strand	P10636

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	143	0.53	0.79	23	empty
2	144	0.52	0.79	24	empty
3	150	0.52	0.79	24	empty
4	156	0.45	0.76	19	empty
5	142	0.43	0.76	20	empty

Interfaces

29 interfaces between chains.

A–E · 2877 Å² buried · 81 hydrogen bonds · protein-protein
B–D · 2877 Å² buried · 80 hydrogen bonds · protein-protein
C–F · 2876 Å² buried · 81 hydrogen bonds · protein-protein
A–H · 2874 Å² buried · 79 hydrogen bonds · protein-protein
C–I · 2867 Å² buried · 78 hydrogen bonds · protein-protein

Compared structures

7QKV · In vitro assembled tau filaments with MgSO4 and NaCl (15a) · 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 7QKV · PDBe 7QKV · UniProt P10636

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