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Structure of the A.THALIANA E1 ufd domain in complex with E2

Analyse Structure of the A.THALIANA E1 ufd domain in complex with E2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6GUM
Type
protein
Length
266 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sumo-conjugating enzyme SCE1; SAE2
EC
2.3.2.-
UniProt
Q42551, A0A178VMI9
Pockets
1 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASumo-conjugating enzyme SCE1 (EC 2.3.2.-)protein15534% helix, 19% strandQ42551
BSAE2protein11122% helix, 32% strandA0A178VMI9

Ligands and binding sites

  • GOL · Glycerol · additive · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1610.380.7912GOL

Interfaces

1 interface between chains.

  • A–B · 929 Ų buried · 15 hydrogen bonds · protein-protein

Compared structures

  • 6GUM · Structure of the A.thaliana E1 UFD domain in complex with E2 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q42551 · AlphaFold monomer V2.0 prediction for sumo-conjugating enzyme SCE1 (Q42551) · a predicted model of the same protein · chain A against A, TM-score 0.98

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