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Doublet tau fibril from corticobasal degeneration human brain tissue

Analyse Doublet tau fibril from corticobasal degeneration human brain tissue in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6VH7
Type
protein
Length
642 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Microtubule-associated protein tau
UniProt
P10636
Pockets
11 · best druggability 0.52

Structure

electron microscopy · 1 distinct chain · 0% helix, 75% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, E, F, GMicrotubule-associated protein tauprotein1070% helix, 75% strandP10636

Pockets

11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12260.520.7731empty
22320.510.7633empty
3620.470.8420empty
4890.460.8121empty
51460.450.7620empty

Interfaces

13 interfaces between chains.

  • E–F · 4447 Ų buried · 165 hydrogen bonds · protein-protein
  • F–G · 4441 Ų buried · 162 hydrogen bonds · protein-protein
  • A–B · 4437 Ų buried · 165 hydrogen bonds · protein-protein
  • B–C · 4432 Ų buried · 162 hydrogen bonds · protein-protein
  • C–G · 141 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 6VH7 · Doublet Tau Fibril from Corticobasal Degeneration Human Brain Tissue · the same entry in another collection · chain A against A, TM-score 1.00

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