PDBe 1zkk

X-ray diffraction
1.45Å resolution

Crystal structure of hSET8 in ternary complex with H4 peptide (16-24) and AdoHcy

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
N-lysine methyltransferase KMT5A Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 167 amino acids
Theoretical weight: 18.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW Q9NQR1 (Residues: 231-393; Coverage: 42%)
Gene names: KMT5A, PRSET7, SET07, SET8, SETD8
Sequence domains: SET domain
Structure domains: SET domain
Histone H4 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 10 amino acids
Theoretical weight: 1.28 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: NEW P62805 (Residues: 16-25; Coverage: 10%)
Gene names: H4/A, H4/B, H4/C, H4/D, H4/E, H4/G, H4/H, H4/I, H4/J, H4/K, H4/M, H4/N, H4/O, H4F2, H4FA, H4FB, H4FC, H4FD, H4FE, H4FG, H4FH, H4FI, H4FJ, H4FK, H4FM, H4FN, H4FO, HIST1H4A, HIST1H4B, HIST1H4C, HIST1H4D, HIST1H4E, HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4L, HIST2H4, HIST2H4A, HIST2H4B, HIST4H4

Ligands and Environments


Cofactor: Ligand SAH 4 x SAH
No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P1
Unit cell:
a: 43.96Å b: 45.775Å c: 94.435Å
α: 89.22° β: 87.07° γ: 90.72°
R-values:
R R work R free
0.206 0.169 0.199
Expression systems:
  • Escherichia coli
  • Not provided