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Ligands
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F2N [(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2r,3s,4s)-5-[7,8-dimethyl-2,4-dioxo-5-(3-phenylpropanoyl)-1,3,4,5-tetrahydrobenzo[G]pteridin-10(2h)-yl]-2,3,4-trihydroxypentyl dihydrogen diphosphate
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Code : 2EJR   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : LSD1-tranylcypromine complex
Release Data : 2008-01-01
Compound :
mol_id molecule chains synonym
1 Lysine-specific histone demethylase 1 A Flavin-containing amine oxidase domain-containing protein 2, BRAF35-HDAC complex protein BHC110
ec: 1.-.-.-
fragment: LSD1, residues 172-833
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: KIAA0601, LSD1
expression_system_vector_type: PLASMID
expression_system_plasmid: p-GEX-6P-1
Authors : Sengoku, T., Mimasu, S., Umehara, T., Yokoyama, S., RIKEN Structural Genomics/Proteomics Initiative (RSGI)
Keywords : Tower domain, LSD1, FAD, Tranylcypromine, Parnate, amine oxidase, histone, demethylase, Alternative splicing, Chromatin regulator, Coiled coil, Nucleus, Oxidoreductase, Phosphorylation, Repressor, Transcription, Transcription regulation, Structural Genomics, NPPSFA, National Project on Protein Structural and Functional Analyses, RIKEN Structural Genomics/Proteomics Initiative, RSGI
Exp. method : X-RAY DIFFRACTION ( 2.70 Å )
Citation :

Crystal structure of histone demethylase LSD1 and tranylcypromine at 2.25A

Mimasu, S.,Sengoku, T.,Fukuzawa, S.  et al.
(2008)  Biochem.Biophys.Res.Commun.  366 : 15 - 22

PubMed: 18039463
DOI: 10.1016/j.bbrc.2007.11.066

Chain : A
UniProt : O60341 (KDM1A_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
2 A + 2 H2O + N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] = 2 AH2 + 2 formaldehyde + L-lysyl(4)-[histone H3] 1.14.99.66 PubMed:15620353, PubMed:15811342
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