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In vitro assembled 297-394 tau filaments in pbs (35D)

Analyse In vitro assembled 297-394 tau filaments in pbs (35D) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QK1
Type: protein
Length: 450 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 4 · best druggability 0.54

Structure

electron microscopy · 1 distinct chain · 0% helix, 63% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C, E, F, A, B, D	Microtubule-associated protein tau	protein	75	0% helix, 63% strand	P10636

Pockets

4 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	173	0.54	0.79	24	empty
2	142	0.52	0.79	25	empty
3	79	0.34	0.75	16	empty
4	54	0.28	0.75	15	empty

Interfaces

11 interfaces between chains.

C–E · 3166 Å² buried · 85 hydrogen bonds · protein-protein
C–F · 3157 Å² buried · 86 hydrogen bonds · protein-protein
A–B · 3152 Å² buried · 88 hydrogen bonds · protein-protein
A–D · 3138 Å² buried · 83 hydrogen bonds · protein-protein
E–B · 118 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7QK1 · In vitro assembled 297-394 tau filaments in PBS (35d) · the same entry in another collection · chain C against C, 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 7QK1 · PDBe 7QK1 · UniProt P10636

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