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Structure of ttr R104H: a non-amyloidogenic variant with protective clinical effects

Analyse Structure of ttr R104H: a non-amyloidogenic variant with protective clinical… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1X7T
Type
protein
Length
225 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transthyretin
UniProt
P02766
Pockets
2 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 53% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATransthyretinprotein1166% helix, 53% strandP02766
BTransthyretinprotein1096% helix, 54% strandP02766

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1930.380.7520empty
2720.310.7416empty

Interfaces

1 interface between chains.

  • A–B · 892 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 1X7T · Structure of TTR R104H: a non-amyloidogenic variant with protective clinical effects · the same entry in another collection · chain A against A, TM-score 1.00

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