3h8k

X-ray diffraction
1.8Å resolution

Crystal structure of Ube2g2 complxed with the G2BR domain of gp78 at 1.8-A resolution

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

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-158052 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Ubiquitin-conjugating enzyme E2 G2 Chain: A
Molecule details ›
Chain: A
Length: 164 amino acids
Theoretical weight: 18.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P60604 (Residues: 2-165; Coverage: 99%)
Gene names: UBC7, UBE2G2
Sequence domains: Ubiquitin-conjugating enzyme
Structure domains: Ubiquitin Conjugating Enzyme
E3 ubiquitin-protein ligase AMFR Chain: B
Molecule details ›
Chain: B
Length: 28 amino acids
Theoretical weight: 3.55 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UKV5 (Residues: 573-600; 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: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 48.92Å b: 60.15Å c: 61.64Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.193 0.242
Expression system: Escherichia coli