X-ray diffraction
2.6Å resolution

C-terminal cysteine-rich domain of human CHFR bound to P(1),P(2)- Diadenosine-5'-pyrophosphate


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
E3 ubiquitin-protein ligase CHFR Chains: A, B
Molecule details ›
Chains: A, B
Length: 261 amino acids
Theoretical weight: 29.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q96EP1 (Residues: 407-664; Coverage: 39%)
Gene names: CHFR, RNF196
Sequence domains:
Structure domains: Herpes Virus-1

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: C2
Unit cell:
a: 163.05Å b: 52.12Å c: 83.61Å
α: 90° β: 105.34° γ: 90°
R R work R free
0.199 0.195 0.246
Expression system: Escherichia coli BL21(DE3)