2l3r

Solution NMR

NMR structure of UHRF1 Tandem Tudor 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-174516 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
E3 ubiquitin-protein ligase UHRF1 Chain: A
Molecule details ›
Chain: A
Length: 162 amino acids
Theoretical weight: 18.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96T88 (Residues: 126-285; Coverage: 20%)
Gene names: ICBP90, NP95, RNF106, UHRF1
Sequence domains: Tandem tudor domain within UHRF1
Structure domains:
Histone H3 Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.29 KDa
Source organism: synthetic construct
Expression system: Not provided
UniProt:
  • Canonical: Q3BDD9 (Residues: 2-12; Coverage: 9%)
Gene name: H3

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 80%
Refinement method: molecular dynamics
Expression systems:
  • Escherichia coli
  • Not provided