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Cryoem structure of the erad-associated E3 ubiquitin-protein ligase HRD1

Analyse Cryoem structure of the erad-associated E3 ubiquitin-protein ligase HRD1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5V6P
Type
protein
Length
540 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Erad-associated E3 ubiquitin-protein ligase HRD1
EC
2.3.2.27
UniProt
Q08109
Pockets
5 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 88% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BErad-associated E3 ubiquitin-protein ligase HRD1 (EC 2.3.2.27)protein27088% helix, 0% strandQ08109

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17950.860.8895empty
25630.750.8247empty
34860.730.8234empty
41530.560.8122empty
5520.310.7511empty

Interfaces

1 interface between chains.

  • A–B · 1812 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5V6P · CryoEM structure of the ERAD-associated E3 ubiquitin-protein ligase HRD1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q08109 · AlphaFold monomer V2.0 prediction for erad-associated E3 ubiquitin- protein ligase HRD1… · a predicted model of the same protein · chain A against A, TM-score 0.93

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