3s8p

X-ray diffraction
1.85Å resolution

Crystal Structure of the SET Domain of Human Histone-Lysine N-Methyltransferase SUV420H1 In Complex With S-Adenosyl-L-Methionine

Released:

Function and Biology Details

Reactions catalysed:
S-adenosyl-L-methionine + a [histone H4]-L-lysine(20) = S-adenosyl-L-homocysteine + a [histone H4]-N(6)-methyl-L-lysine(20)
S-adenosyl-L-methionine + a [histone H4]-N(6)-methyl-L-lysine(20) = S-adenosyl-L-homocysteine + a [histone H4]-N(6),N(6)-dimethyl-L-lysine(20)
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase KMT5B Chains: A, B
Molecule details ›
Chains: A, B
Length: 273 amino acids
Theoretical weight: 31.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4FZB7 (Residues: 63-335; Coverage: 31%)
Gene names: CGI-85, KMT5B, SUV420H1
Sequence domains: SET domain
Structure domains:

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P1
Unit cell:
a: 46.424Å b: 50.134Å c: 74.839Å
α: 100.99° β: 108.05° γ: 89.76°
R-values:
R R work R free
0.188 0.187 0.212
Expression system: Escherichia coli