› 4gu1

X-ray diffraction
2.94Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) a [histone H3]-N(6),N(6)-dimethyl-L-lysine(4) + acceptor + H(2)O = a [histone H3]-N(6)-methyl-L-lysine(4) + formaldehyde + reduced acceptor
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-185462 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysine-specific histone demethylase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 784 amino acids
Theoretical weight: 88.1 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q8NB78 (Residues: 51-822; Coverage: 94%)
Gene names: AOF1, C6orf193, KDM1B, LSD2
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand FAD 2 x FAD
Ligand CL 4 x CL
Ligand NA 2 x NA
Ligand ZN 6 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 89.163Å b: 89.216Å c: 342.538Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.228
Expression system: Spodoptera frugiperda

Quick links

Citations

20 review citations

Histone lysine demethylases as targets for anticancer therapy.
Højfeldt et al. (2013)
19 more

2 mentions without citation

Structure and function of dioxygenases in histone demethylation and DNA/RNA demethylation.
Dong et al. (2014)
1 more