4g3o

X-ray diffraction
1.6Å resolution

Crystal structure of the CUE domain of the E3 ubiquitin ligase AMFR (gp78)

Released:
Source organism: Homo sapiens
Entry authors: Kozlov G, LePage K, Gehring K

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase AMFR Chain: A
Molecule details ›
Chain: A
Length: 58 amino acids
Theoretical weight: 6.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9UKV5 (Residues: 456-498; Coverage: 7%)
Gene names: AMFR, RNF45
Sequence domains: CUE domain
Structure domains: DNA helicase RuvA subunit, C-terminal domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F1
Spacegroup: P65
Unit cell:
a: 55.396Å b: 55.396Å c: 30.993Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.161 0.159 0.186
Expression system: Escherichia coli BL21