3fsh

X-ray diffraction
2.76Å resolution

Crystal structure of the ubiquitin conjugating enzyme Ube2g2 bound to the G2BR domain of ubiquitin ligase gp78

Released:

Function and Biology Details

Reactions catalysed:
S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-cysteine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-S-ubiquitinyl-L-cysteine

Structure analysis Details

Assemblies composition:
monomeric
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-158056 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-conjugating enzyme E2 G2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 168 amino acids
Theoretical weight: 18.86 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P60605 (Residues: 1-165; Coverage: 100%)
Gene names: Ubc7, Ube2g2
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
E3 ubiquitin-protein ligase AMFR Chain: C
Molecule details ›
Chain: C
Length: 28 amino acids
Theoretical weight: 3.45 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9UKV5 (Residues: 574-601; Coverage: 4%)
Gene names: AMFR, RNF45
Sequence domains: E3 gp78 Ube2g2-binding region (G2BR)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P43212
Unit cell:
a: 105.719Å b: 105.719Å c: 142.855Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.216 0.216 0.256
Expression systems:
  • Escherichia coli
  • Not provided