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E3 ring ligase binding domain

Analyse E3 ring ligase binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OVX
Type
protein
Length
186 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
E3 ubiquitin-protein ligase TRIM7; Peptide G
EC
2.3.2.27
UniProt
Q9C029
Pockets
1 · best druggability 0.30

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AE3 ubiquitin-protein ligase TRIM7 (EC 2.3.2.27)protein1743% helix, 43% strandQ9C029
QPeptide Gprotein1267% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1780.300.7316empty

Interfaces

1 interface between chains.

  • A–Q · 490 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 7OVX · E3 RING ligase binding domain · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9C029 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase TRIM7 (Q9C029) · a predicted model of the same protein · chain A against A, TM-score 0.98

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