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Crystal structure of the catalytic domain of human ubiquitin ligase AREL1

Analyse Crystal structure of the catalytic domain of human ubiquitin ligase AREL1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LOH
Type
protein
Length
1,120 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Apoptosis-resistant E3 ubiquitin protein ligase 1
EC
2.3.2.26
UniProt
O15033
Pockets
17 · best druggability 0.81

Structure

x-ray diffraction · 3 distinct chains · 50% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AApoptosis-resistant E3 ubiquitin protein ligase 1 (EC 2.3.2.26)protein37349% helix, 13% strandO15033
BApoptosis-resistant E3 ubiquitin protein ligase 1 (EC 2.3.2.26)protein37551% helix, 13% strandO15033
CApoptosis-resistant E3 ubiquitin protein ligase 1 (EC 2.3.2.26)protein37249% helix, 11% strandO15033

Pockets

17 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111110.810.82112empty
24720.730.8242empty
36270.690.7746empty
43400.610.7834empty
5810.570.8720empty

Interfaces

3 interfaces between chains.

  • B–C · 1048 Ų buried · 2 hydrogen bonds · protein-protein
  • A–B · 540 Ų buried · 5 hydrogen bonds · protein-protein
  • A–C · 507 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 6LOH · Crystal structure of the catalytic domain of human ubiquitin ligase AREL1 · the same entry in another collection · chain A against A, TM-score 1.00
  • O15033 · AlphaFold monomer V2.0 prediction for apoptosis-resistant E3 ubiquitin protein ligase 1… · a predicted model of the same protein · chain B against A, TM-score 0.98

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