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Crystal structure of the uba domain from edd ubiquitin ligase in complex with ubiquitin

Analyse Crystal structure of the uba domain from edd ubiquitin ligase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2QHO
Type
protein
Length
488 residues
Chains
8
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin; E3 ubiquitin-protein ligase EDD1
EC
6.3.2.-
UniProt
P62990, O95071
Pockets
3 · best druggability 0.65

Structure

x-ray diffraction · 7 distinct chains · 45% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, GUbiquitinprotein7226% helix, 36% strandP62990
BE3 ubiquitin-protein ligase EDD1 (EC 6.3.2.-)protein4768% helix, 0% strandO95071
CUbiquitinprotein7624% helix, 34% strandP62990
DE3 ubiquitin-protein ligase EDD1 (EC 6.3.2.-)protein4967% helix, 0% strandO95071
EUbiquitinprotein7524% helix, 35% strandP62990
FE3 ubiquitin-protein ligase EDD1 (EC 6.3.2.-)protein4971% helix, 0% strandO95071
HE3 ubiquitin-protein ligase EDD1 (EC 6.3.2.-)protein4869% helix, 0% strandO95071

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15100.650.7753empty
21090.460.7922empty
3920.320.7321empty

Interfaces

11 interfaces between chains.

  • E–F · 641 Ų buried · 9 hydrogen bonds · protein-protein
  • C–D · 563 Ų buried · 4 hydrogen bonds · protein-protein
  • A–B · 551 Ų buried · 7 hydrogen bonds · protein-protein
  • G–H · 540 Ų buried · 8 hydrogen bonds · protein-protein
  • A–E · 326 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 2QHO · Crystal structure of the UBA domain from EDD ubiquitin ligase in complex with ubiquitin · the same entry in another collection · chain A against A, TM-score 1.00

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