› 2uxx

X-ray diffraction
2.74Å resolution

Human LSD1 Histone Demethylase-CoREST in complex with an FAD- tranylcypromine adduct

Released:
DOI: 10.2210/pdb2uxx/pdb
PDB entry 2uxx coloured by chain, front view.
PDB entry 2uxx coloured by chain, side view.
PDB entry 2uxx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the inhibition of the LSD1 histone demethylase by the antidepressant trans-2-phenylcyclopropylamine.
Yang M, Culhane JC, Szewczuk LM, Jalili P, Ball HL, Machius M, Cole PA, Yu H
Biochemistry 46 8058-65 (2007)
PMID: 17569509

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 domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129967 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lysine-specific histone demethylase 1A Chain: A
Molecule details ›
Chain: A
Length: 666 amino acids
Theoretical weight: 74.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O60341 (Residues: 171-836; Coverage: 78%)
Gene names: AOF2, KDM1, KDM1A, KIAA0601, LSD1
Sequence domains:
Structure domains:
REST corepressor 1 Chain: B
Molecule details ›
Chain: B
Length: 235 amino acids
Theoretical weight: 26.43 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9UKL0 (Residues: 289-485; Coverage: 41%)
Gene names: KIAA0071, RCOR, RCOR1
Sequence domains:
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1

Ligands and Environments

3 bound ligands:
Ligand FAJ 1 x FAJ
Ligand GOL 2 x GOL
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I222
Unit cell:
a: 120.798Å b: 178.5Å c: 235.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.236 0.235 0.26
Expression system: Escherichia coli BL21

Quick links

Citations

51 review citations

Reversal of histone methylation: biochemical and molecular mechanisms of histone demethylases.
Mosammaparast et al. (2010)
50 more

12 mentions without citation

LSD1/KDM1A inhibitors in clinical trials: advances and prospects.
Fang et al. (2019)
11 more