MolNFT v1 · #185901 · protein

In vitro assembled 0N4R tau filaments with phosphoserine (47A)

7QKY · Microtubule-associated protein tau: “In vitro assembled 0N4R tau filaments with phosphoserine (47A)”. Electron microscopy, 1 pocket (best druggability 0.41). MolNFT v1 #185901 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 7QKY
Type: protein
Length: 396 residues
Chains: 6
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Microtubule-associated protein tau
UniProt: P10636
Pockets: 1 · best druggability 0.41

Structure

electron microscopy · 1 distinct chain · 0% helix, 61% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F	Microtubule-associated protein tau	protein	66	0% helix, 61% strand	P10636

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	147	0.41	0.74	31	empty

Interfaces

12 interfaces between chains.

D–F · 2639 Å² buried · 89 hydrogen bonds · protein-protein
C–D · 2635 Å² buried · 95 hydrogen bonds · protein-protein
A–B · 2634 Å² buried · 90 hydrogen bonds · protein-protein
B–E · 2627 Å² buried · 90 hydrogen bonds · protein-protein
B–C · 554 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

7QKY · In vitro assembled 0N4R tau filaments with phosphoserine (47a) · 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 7QKY · PDBe 7QKY · UniProt P10636

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