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Transthyritin derived amyloid fibril from patient with hereditary V30M attr amyloidosis

Analyse Transthyritin derived amyloid fibril from patient with hereditary V30M attr… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SDZ
Type
protein
Length
1,012 residues
Chains
11
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transthyretin
UniProt
P02766
Pockets
4 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 0% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, KTransthyretinprotein920% helix, 53% strandP02766

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18430.860.8999empty
22490.830.9556empty
32670.800.9262empty
41200.440.7731empty

Interfaces

19 interfaces between chains.

  • E–F · 3894 Ų buried · 128 hydrogen bonds · protein-protein
  • J–K · 3886 Ų buried · 141 hydrogen bonds · protein-protein
  • B–C · 3878 Ų buried · 131 hydrogen bonds · protein-protein
  • F–G · 3876 Ų buried · 130 hydrogen bonds · protein-protein
  • A–B · 3871 Ų buried · 140 hydrogen bonds · protein-protein

Compared structures

  • 6SDZ · transthyritin derived amyloid fibril from patient with hereditary V30M ATTR amyloidosis · the same entry in another collection · chain A against A, TM-score 1.00

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