› 3zn0

X-ray diffraction
2.8Å 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

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-129954 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Lysine-specific histone demethylase 1A Chain: A
Molecule details ›
Chain: A
Length: 872 amino acids
Theoretical weight: 94.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O60341 (Residues: 1-173, 174-852; Coverage: 100%)
Gene names: AOF2, KDM1, KDM1A, KIAA0601, LSD1
Sequence domains:
Structure domains:
REST corepressor 1 Chain: B
Molecule details ›
Chain: B
Length: 482 amino acids
Theoretical weight: 53.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9UKL0 (Residues: 4-485; Coverage: 99%)
Gene names: KIAA0071, RCOR, RCOR1
Sequence domains:
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1
PEPTIDE Chain: C
Molecule details ›
Chain: C
Length: 6 amino acids
Theoretical weight: 649 Da
Source organism: Homo sapiens
Expression system: Escherichia coli BL21

Ligands and Environments

1 bound ligand:
Ligand FAD 1 x FAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: I222
Unit cell:
a: 119.91Å b: 180.38Å c: 234.139Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.229 0.244
Expression system: Escherichia coli BL21

Quick links

Citations

11 review citations

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

2 mentions without citation

Structural insight into inhibitors of flavin adenine dinucleotide-dependent lysine demethylases.
Niwa et al. (2017)
1 more