3sox

X-ray diffraction
2.65Å resolution

Structure of UHRF1 PHD finger in the free form

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

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase UHRF1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 70 amino acids
Theoretical weight: 7.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96T88 (Residues: 298-367; Coverage: 9%)
Gene names: ICBP90, NP95, RNF106, UHRF1
Sequence domains: PHD-finger
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: I212121
Unit cell:
a: 53.746Å b: 53.805Å c: 128.476Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.248 0.294
Expression system: Escherichia coli BL21(DE3)