6bp4

X-ray diffraction
2.77Å resolution

Structure of the S. pombe Clr4 catalytic domain bound to SAM

Released:
Model geometry
Fit model/data

Function and Biology Details

Reactions 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)
S-adenosyl-L-methionine + a [histone H3]-N(6),N(6)-dimethyl-L-lysine(9) = S-adenosyl-L-homocysteine + a [histone H3]-N(6),N(6),N(6)-trimethyl-L-lysine(9)
S-adenosyl-L-methionine + a [histone H3]-L-lysine(9) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(9)
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-129896 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase, H3 lysine-9 specific Chains: A, B
Molecule details ›
Chains: A, B
Length: 303 amino acids
Theoretical weight: 34.25 KDa
Source organism: Schizosaccharomyces pombe 972h-
Expression system: Escherichia coli
UniProt:
  • Canonical: O60016 (Residues: 192-490; Coverage: 61%)
Gene names: SPBC428.08c, clr4, kmt1
Sequence domains:
Structure domains: SET domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2
Unit cell:
a: 131.919Å b: 71.04Å c: 96.674Å
α: 90° β: 125.06° γ: 90°
R-values:
R R work R free
0.225 0.223 0.264
Expression system: Escherichia coli