X-ray diffraction
2.25Å resolution

Crystal structure of Lysine-specific histone demethylase 1

Source organism: Homo sapiens
Primary publication:
Crystal structure of histone demethylase LSD1 and tranylcypromine at 2.25 A.
Biochem. Biophys. Res. Commun. 366 15-22 (2008)
PMID: 18039463

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Lysine-specific histone demethylase 1A Chain: A
Molecule details ›
Chain: A
Length: 662 amino acids
Theoretical weight: 73.65 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
  • Canonical: O60341 (Residues: 172-833; Coverage: 78%)
Gene names: AOF2, KDM1, KDM1A, KIAA0601, LSD1
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P6122
Unit cell:
a: 185.759Å b: 185.759Å c: 108.742Å
α: 90° β: 90° γ: 120°
R R work R free
0.225 0.225 0.254
Expression system: Escherichia coli BL21