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Crystal structure of the auto-inhibited NEDD4 family E3 ligase itch

Analyse Crystal structure of the auto-inhibited NEDD4 family E3 ligase itch in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5XMC
Type
protein
Length
409 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin-protein ligase itchy
EC
2.3.2.26
UniProt
Q8C863
Pockets
3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AE3 ubiquitin-protein ligase itchy (EC 2.3.2.26)protein40946% helix, 16% strandQ8C863

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18470.780.8188empty
22170.700.8631empty
3690.290.7317empty

Compared structures

  • 5XMC · Crystal structure of the auto-inhibited Nedd4 family E3 ligase Itch · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8C863 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase itchy (Q8C863) · a predicted model of the same protein · chain A against A, TM-score 0.96

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