› 1peg

X-ray diffraction
2.59Å resolution

Structural basis for the product specificity of histone lysine methyltransferases

Released:
DOI: 10.2210/pdb1peg/pdb
PDB entry 1peg coloured by chain, front view.
PDB entry 1peg coloured by chain, side view.
PDB entry 1peg coloured by chain, top view.
Source organisms:
Primary publication:
Structural basis for the product specificity of histone lysine methyltransferases.
Zhang X, Yang Z, Khan SI, Horton JR, Tamaru H, Selker EU, Cheng X
Mol Cell 12 177-85 (2003)
PMID: 12887903

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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159428 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 302 amino acids
Theoretical weight: 34.11 KDa
Source organism: Neurospora crassa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8X225 (Residues: 30-331; Coverage: 91%)
Gene names: 29E8.110, NCU04402, dim-5
Sequence domains:
Structure domains: SET domain
Histone H3.1 Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 15 amino acids
Theoretical weight: 1.57 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 2-16; Coverage: 11%)
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

2 bound ligands:
Ligand ZN 8 x ZN
Ligand SAH 2 x SAH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 68.26Å b: 94.17Å c: 114.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.32
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

51 review citations

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

33 mentions without citation

The SET-domain protein superfamily: protein lysine methyltransferases.
Dillon et al. (2005)
32 more