› 3fl2

X-ray diffraction
1.75Å resolution

Crystal structure of the ring domain of the E3 ubiquitin-protein ligase UHRF1

Released:
DOI: 10.2210/pdb3fl2/pdb
PDB entry 3fl2 coloured by chain, front view.
PDB entry 3fl2 coloured by chain, side view.
PDB entry 3fl2 coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Walker JR, Avvakumov GV, Xue S, Li Y, Bountra C, Weigelt J, Arrowsmith CH, Edwards AM, Bochkarev A, Dhe-Paganon S, Structural Genomics Consortium (SGC)

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-572620 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase UHRF1 Chain: A
Molecule details ›
Chain: A
Length: 124 amino acids
Theoretical weight: 14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96T88 (Residues: 672-793; Coverage: 15%)
Gene names: ICBP90, NP95, RNF106, UHRF1
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 45.736Å b: 46.916Å c: 48.409Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.183 0.25
Expression system: Escherichia coli

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