Solution NMR

SET domain of RIZ1 tumor suppressor (PRDM2)

Source organism: Homo sapiens
Primary publication:
Structural studies of the SET domain from RIZ1 tumor suppressor.
Biochem. Biophys. Res. Commun. 366 807-13 (2008)
PMID: 18082620

Function and Biology Details

Reaction catalysed:
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(9) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(9)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
PR domain zinc finger protein 2 Chain: A
Molecule details ›
Chain: A
Length: 163 amino acids
Theoretical weight: 18.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q13029 (Residues: 1-161; Coverage: 9%)
Gene names: KMT8, PRDM2, RIZ
Sequence domains: SET domain
Structure domains: SET domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli