› 2f69

X-ray diffraction
1.3Å resolution

Ternary complex of SET7/9 bound to AdoHcy and a TAF10 peptide

Released:
DOI: 10.2210/pdb2f69/pdb
PDB entry 2f69 coloured by chain, front view.
PDB entry 2f69 coloured by chain, side view.
PDB entry 2f69 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the methylation site specificity of SET7/9.
Couture JF, Collazo E, Hauk G, Trievel RC
Nat Struct Mol Biol 13 140-6 (2006)
PMID: 16415881

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171459 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-lysine N-methyltransferase SETD7 Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 29.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8WTS6 (Residues: 110-366; Coverage: 70%)
Gene names: KIAA1717, KMT7, SET7, SET9, SETD7
Sequence domains:
Structure domains:
Transcription initiation factor TFIID subunit 10 Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.27 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q12962 (Residues: 186-195; Coverage: 5%)
Gene names: TAF10, TAF2A, TAF2H, TAFII30

Ligands and Environments

1 bound ligand:
Ligand SAH 1 x SAH
1 modified residue:
Ligand MLZ 1 x MLZ

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P3221
Unit cell:
a: 83.38Å b: 83.38Å c: 95.52Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.15 0.149 0.174
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

22 review citations

S-adenosyl-methionine-dependent methyltransferases: highly versatile enzymes in biocatalysis, biosynthesis and other biotechnological applications.
Struck et al. (2012)
21 more

8 mentions without citation

Histone lysine methylation dynamics: establishment, regulation, and biological impact.
Black et al. (2012)
7 more