› 1o9s

X-ray diffraction
1.75Å resolution

Crystal structure of a ternary complex of the human histone methyltransferase SET7/9

Released:
DOI: 10.2210/pdb1o9s/pdb
PDB entry 1o9s coloured by chain, front view.
PDB entry 1o9s coloured by chain, side view.
PDB entry 1o9s coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and catalytic mechanism of the human histone methyltransferase SET7/9.
Xiao B, Jing C, Wilson JR, Walker PA, Vasisht N, Kelly G, Howell S, Taylor IA, Blackburn GM, Gamblin SJ
Nature 421 652-6 (2003)
PMID: 12540855

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-159426 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-lysine N-methyltransferase SETD7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 259 amino acids
Theoretical weight: 28.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WTS6 (Residues: 108-366; Coverage: 71%)
Gene names: KIAA1717, KMT7, SET7, SET9, SETD7
Sequence domains:
Structure domains:
Histone H3.1 Chains: K, L
Molecule details ›
Chains: K, L
Length: 10 amino acids
Theoretical weight: 1.24 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 2-11; Coverage: 7%)
Gene names: H3C1, H3C10, H3C11, H3C12, H3C2, H3C3, H3C4, H3C6, H3C7, H3C8, H3FA, H3FB, H3FC HIST1H3C, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

Ligands and Environments

1 bound ligand:
Ligand SAH 2 x SAH
1 modified residue:
Ligand MLZ 2 x MLZ

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 52.69Å b: 75.438Å c: 69.099Å
α: 90° β: 94.16° γ: 90°
R-values:
R R work R free
0.206 0.205 0.222
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

53 review citations

Regulation of chromatin by histone modifications.
Bannister et al. (2011)
52 more

35 mentions without citation

Many paths to methyltransfer: a chronicle of convergence.
Schubert et al. (2003)
34 more