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Cryo-EM structure of a twisted-dimer transthyretin amyloid fibril from vitreous body of the eye

Analyse Cryo-EM structure of a twisted-dimer transthyretin amyloid fibril from vitreous… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OB4
Type
protein
Length
1,288 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transthyretin
UniProt
P02766
Pockets
6 · best druggability 0.82

Structure

electron microscopy · 1 distinct chain · 0% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
G, I, H, J, K, M, L, N, A, B, C, E, D, FTransthyretinprotein920% helix, 46% strandP02766

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17020.820.8670empty
27660.810.8468empty
33440.550.7540empty
44120.550.7343empty
51070.450.7921empty

Interfaces

40 interfaces between chains.

  • A–C · 3928 Ų buried · 128 hydrogen bonds · protein-protein
  • B–D · 3919 Ų buried · 128 hydrogen bonds · protein-protein
  • C–E · 3888 Ų buried · 125 hydrogen bonds · protein-protein
  • G–I · 3878 Ų buried · 121 hydrogen bonds · protein-protein
  • H–F · 3869 Ų buried · 123 hydrogen bonds · protein-protein

Compared structures

  • 7OB4 · Cryo-EM structure of a twisted-dimer transthyretin amyloid fibril from vitreous body of… · the same entry in another collection · chain G against G, TM-score 1.00

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