› 4xdo

X-ray diffraction
1.97Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) a [histone H3]-N(6),N(6),N(6)-trimethyl-L-lysine(9) + 2-oxoglutarate + O(2) = a [histone H3]-N(6),N(6)-dimethyl-L-lysine(9) + succinate + formaldehyde + CO(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190586 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysine-specific demethylase 4C Chains: A, B
Molecule details ›
Chains: A, B
Length: 338 amino acids
Theoretical weight: 39.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H3R0 (Residues: 10-347; Coverage: 32%)
Gene names: GASC1, JHDM3C, JMJD2C, KDM4C, KIAA0780
Sequence domains:
Structure domains: Cupin

Ligands and Environments

6 bound ligands:
Ligand ZN 2 x ZN
Ligand FE 2 x FE
Ligand OGA 2 x OGA
Ligand PGE 2 x PGE
Ligand EDO 1 x EDO
Ligand PG4 1 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: C2
Unit cell:
a: 93.93Å b: 89.77Å c: 98.46Å
α: 90° β: 96.49° γ: 90°
R-values:
R R work R free
0.203 0.2 0.254
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Pharmacological Inhibition of LSD1 for Cancer Treatment.
Yang et al. (2018)
5 more

1 mention without citation

Allele-Specific Chemical Rescue of Histone Demethylases Using Abiotic Cofactors.
Scott et al. (2022)