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3ABT

Crystal Structure of LSD1 in complex with trans-2-pentafluorophenylcyclopropylamine

Summary for 3ABT
Entry DOI10.2210/pdb3abt/pdb
Related2dw4 2uxx 2z5u 3abu
DescriptorLysine-specific histone demethylase 1, [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl (2R,3S,4S)-2,3,4-trihydroxy-5-[(1R,3R,3aS)-1-hydroxy-10,11-dimethyl-4,6-dioxo-3-(pentafluorophenyl)-2,3,5,6-tetrahydro-1H-benzo[g]pyrrolo[2,1-e]pteridin-8(4H)-yl]pentyl dihydrogen diphosphate (2 entities in total)
Functional Keywordsamine oxidase, histone demethylase, tower domain, h3k4, structural genomics, riken structural genomics/proteomics initiative, rsgi, chromatin regulator, developmental protein, fad, nucleus, oxidoreductase, phosphoprotein, repressor, transcription, transcription regulation, nppsfa, national project on protein structural and functional analyses
Biological sourceHomo sapiens (human)
Cellular locationNucleus : O60341
Total number of polymer chains1
Total formula weight74661.92
Authors
Mimasu, S.,Umezawa, N.,Sato, S.,Higuchi, T.,Umehara, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2009-12-21, release date: 2010-07-07, Last modification date: 2023-11-01)
Primary citationMimasu, S.,Umezawa, N.,Sato, S.,Higuchi, T.,Umehara, T.,Yokoyama, S.
Structurally Designed trans-2-Phenylcyclopropylamine Derivatives Potently Inhibit Histone Demethylase LSD1/KDM1
Biochemistry, 49:6494-6503, 2010
Cited by
PubMed: 20568732
DOI: 10.1021/bi100299r
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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