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Protease-associated domain of the E3 ligase grail

Analyse Protease-associated domain of the E3 ligase grail in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3ICU
Type
protein
Length
171 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin-protein ligase RNF128
EC
6.3.2.-
UniProt
Q8TEB7
Ligands
NAG

Structure

x-ray diffraction · 1 distinct chain · 13% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AE3 ubiquitin-protein ligase RNF128 (EC 6.3.2.-)protein17113% helix, 35% strandQ8TEB7

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A

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

Modifications

Observed in the structure: 1 glycan (N-glycosylation).

Compared structures

  • 3ICU · Protease-associated domain of the E3 ligase grail · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8TEB7 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase RNF128 (Q8TEB7) · a predicted model of the same protein · chain A against A, TM-score 0.96

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