GL1X · GenesisL1 explorer

Research workbench

Structure of TSC1 ntd and linker domain

Analyse Structure of TSC1 ntd and linker domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7A0N
Type
protein
Length
1,551 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uncharacterized PROTEIN,UNCHARACTERIZED protein
UniProt
G0S5K3
Pockets
20 · best druggability 0.74

Structure

x-ray diffraction · 4 distinct chains · 74% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUncharacterized PROTEIN,UNCHARACTERIZED proteinprotein39374% helix, 1% strandG0S5K3
BUncharacterized PROTEIN,UNCHARACTERIZED proteinprotein39272% helix, 1% strandG0S5K3
CUncharacterized PROTEIN,UNCHARACTERIZED proteinprotein38073% helix, 1% strandG0S5K3
DUncharacterized PROTEIN,UNCHARACTERIZED proteinprotein38675% helix, 1% strandG0S5K3

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15800.740.8170empty
25470.710.8052empty
34020.670.7941empty
44110.640.7847empty
53220.630.7946empty

Interfaces

3 interfaces between chains.

  • B–D · 1752 Ų buried · 21 hydrogen bonds · protein-protein
  • A–B · 1028 Ų buried · 8 hydrogen bonds · protein-protein
  • C–D · 1021 Ų buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 28 modified (engineered).

Compared structures

  • 7A0N · Structure of TSC1 NTD and linker domain · 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.