4ft2

X-ray diffraction
3.2Å resolution

crystal structure of Zea mays ZMET2 in complex H3(1-15)K9me2 peptide and SAH

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + DNA = S-adenosyl-L-homocysteine + DNA containing 5-methylcytosine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-159439 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA (cytosine-5)-methyltransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 784 amino acids
Theoretical weight: 87.59 KDa
Source organism: Zea mays
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9AXT8 (Residues: 130-912; Coverage: 86%)
Gene name: MET2A
Sequence domains:
Structure domains:
Histone H3.1 Chain: P
Molecule details ›
Chain: P
Length: 15 amino acids
Theoretical weight: 1.59 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


Cofactor: Ligand SAH 2 x SAH
No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P1
Unit cell:
a: 64.861Å b: 88.858Å c: 113.501Å
α: 93.15° β: 95.72° γ: 110.7°
R-values:
R R work R free
0.237 0.235 0.277
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided