2e6s

Solution NMR

Solution structure of the PHD domain in RING finger protein 107

Released:
Source organism: Homo sapiens
Entry authors: Kadirvel S, He F, Muto Y, Inoue M, Kigawa T, Shirouzu M, Terada T, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

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)
PDBe Complex ID:
PDB-CPX-188676 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
E3 ubiquitin-protein ligase UHRF2 Chain: A
Molecule details ›
Chain: A
Length: 77 amino acids
Theoretical weight: 8.52 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q96PU4 (Residues: 326-395; Coverage: 9%)
Gene names: NIRF, RNF107, UHRF2
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
Refinement method: torsion angle dynamics
Expression system: Not provided