› 5ttg

X-ray diffraction
1.66Å resolution

Crystal structure of catalytic domain of GLP with MS012

Released:
DOI: 10.2210/pdb5ttg/pdb
PDB entry 5ttg coloured by chain, front view.
PDB entry 5ttg coloured by chain, side view.
PDB entry 5ttg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery of Potent and Selective Inhibitors for G9a-Like Protein (GLP) Lysine Methyltransferase.
Xiong Y, Li F, Babault N, Dong A, Zeng H, Wu H, Chen X, Arrowsmith CH, Brown PJ, Liu J, Vedadi M, Jin J
J Med Chem 60 1876-1891 (2017)
PMID: 28135087

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + a [histone H3]-L-lysine(9) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(9)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190698 (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:
Structure domains: SET domain

Ligands and Environments

7 bound ligands:
Ligand SAM 2 x SAM
Ligand 7KZ 2 x 7KZ
Ligand ZN 8 x ZN
Ligand CL 1 x CL
Ligand GOL 1 x GOL
Ligand UNX 15 x UNX
Ligand DMS 1 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 74.429Å b: 95.9Å c: 102.113Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.171 0.192
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

PROTACs: An Emerging Therapeutic Modality in Precision Medicine.
Nalawansha et al. (2020)
4 more

7 mentions without citation

Inhibitors of Protein Methyltransferases and Demethylases.
Kaniskan et al. (2018)
6 more