GL1X · GenesisL1 explorer

Research workbench

Neutron structure of human transthyretin (ttr) at room temperature to 2.0A resolution (laue)

Analyse Neutron structure of human transthyretin (ttr) at room temperature to 2.0A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4PVM
Type
protein
Length
233 residues
Chains
2
Method
neutron diffraction; x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transthyretin
UniProt
P02766
Pockets
2 · best druggability 0.33

Structure

neutron diffraction; x-ray diffraction · 2 distinct chains · 6% helix, 52% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATransthyretinprotein1166% helix, 53% strandP02766
BTransthyretinprotein1176% helix, 52% strandP02766

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1720.330.7615empty
2570.290.7513empty

Interfaces

1 interface between chains.

  • A–B · 917 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 4PVM · Neutron structure of human transthyretin (TTR) at room temperature to 2.0A resolution… · the same entry in another collection · chain B against B, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.