2xoc

X-ray diffraction
1.89Å resolution

C-terminal cysteine-rich domain of human CHFR bound to mADPr

Released:

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 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)
UniProt:
  • Canonical: Q96EP1 (Residues: 407-664; Coverage: 39%)
Gene names: CHFR, RNF196
Sequence domains:
Structure domains: Herpes Virus-1

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: C2
Unit cell:
a: 161.54Å b: 51.7Å c: 82.36Å
α: 90° β: 105.76° γ: 90°
R-values:
R R work R free
0.17 0.168 0.194
Expression system: Escherichia coli BL21(DE3)