PDBe 5v9j

X-ray diffraction
1.74Å resolution

Crystal structure of catalytic domain of GLP with MS0105

Released:
Source organism: Homo sapiens
Entry authors: Dong A, Zeng H, Liu J, Xiong Y, Babault N, Jin J, Tempel W, Bountra C, Arrowsmith CH, Edwards AM, Wu H, Brown PJ, Structural Genomics Consortium (SGC)

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:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase EHMT1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 287 amino acids
Theoretical weight: 32.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9H9B1 (Residues: 982-1266; Coverage: 22%)
Gene names: EHMT1, EUHMTASE1, GLP, KIAA1876, KMT1D
Sequence domains:

Ligands and Environments


Cofactor: Ligand SAM 2 x SAM

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 74.848Å b: 95.891Å c: 102.416Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.197
Expression system: Escherichia coli BL21