GL1X · GenesisL1 explorer

Research workbench

Viral capsid protein shp at pH 5.5

Analyse Viral capsid protein shp at pH 5.5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TD0
Type
protein
Length
408 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Head decoration protein
UniProt
P36275
Pockets
4 · best druggability 0.38

Structure

x-ray diffraction · 3 distinct chains · 5% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHead decoration proteinprotein1025% helix, 36% strandP36275
CHead decoration proteinprotein1015% helix, 37% strandP36275
DHead decoration proteinprotein1035% helix, 36% strandP36275

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11150.380.7522empty
2550.380.8016empty
3560.350.7818empty
4520.330.7817empty

Interfaces

3 interfaces between chains.

  • A–B · 676 Ų buried · 4 hydrogen bonds · protein-protein
  • C–D · 646 Ų buried · 3 hydrogen bonds · protein-protein
  • A–C · 160 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1TD0 · Viral capsid protein SHP at pH 5.5 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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