X-ray diffraction
2Å resolution

Crystal structure of RBBP4 in complex with PRDM16 N-terminal peptide


Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + a [histone H3]-L-lysine(9) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(9)

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-binding protein RBBP4 Chains: A, C
Molecule details ›
Chains: A, C
Length: 427 amino acids
Theoretical weight: 47.85 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
  • Canonical: Q09028 (Residues: 1-425; Coverage: 100%)
Gene names: RBAP48, RBBP4
Sequence domains:
Structure domains: YVTN repeat-like/Quinoprotein amine dehydrogenase
Histone-lysine N-methyltransferase PRDM16 Chains: B, D
Molecule details ›
Chains: B, D
Length: 12 amino acids
Theoretical weight: 1.42 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: Q9HAZ2 (Residues: 1-12; Coverage: 1%)
Gene names: KIAA1675, MEL1, PFM13, PRDM16

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 76.034Å b: 59.862Å c: 101.843Å
α: 90° β: 94.55° γ: 90°
R R work R free
0.2 0.199 0.233
Expression systems:
  • Spodoptera frugiperda
  • Not provided