2lgk

Solution NMR

NMR Structure of UHRF1 PHD domains in a complex with histone H3 peptide

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:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-162891 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase UHRF1 Chain: A
Molecule details ›
Chain: A
Length: 69 amino acids
Theoretical weight: 7.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96T88 (Residues: 298-366; Coverage: 9%)
Gene names: ICBP90, NP95, RNF106, UHRF1
Sequence domains: PHD-finger
Structure domains: Zinc/RING finger domain, C3HC4 (zinc finger)
histone H3 peptide Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.35 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 79%
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli
  • Not provided