GL1X · GenesisL1 explorer

Research workbench

Catalytic domain of the human E3 ubiquitin-protein ligase HUWE1

Analyse Catalytic domain of the human E3 ubiquitin-protein ligase HUWE1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3G1N
Type
protein
Length
745 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin-protein ligase HUWE1
EC
6.3.2.-
UniProt
Q7Z6Z7
Ligands
NA
Pockets
9 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AE3 ubiquitin-protein ligase HUWE1 (EC 6.3.2.-)protein37447% helix, 14% strandQ7Z6Z7
BE3 ubiquitin-protein ligase HUWE1 (EC 6.3.2.-)protein37149% helix, 15% strandQ7Z6Z7

Ligands and binding sites

  • NA · Sodium ion · metal · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

9 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16240.780.8459empty
29480.760.7861empty
34470.700.8140empty
44530.670.7938empty
52450.630.8235empty

Interfaces

1 interface between chains.

  • A–B · 1473 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

  • 3G1N · Catalytic domain of the human E3 ubiquitin-protein ligase HUWE1 · 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.