2UXN: Lysine-specific histone demethylase 1

Structural Basis of Histone Demethylation by LSD1 Revealed by Suicide Inactivation. Determined by X-ray diffraction at 2.72 Å resolution. Released 29 May 2007.

Method
X-ray diffraction
Resolution
2.72 Å
Organism
HOMO SAPIENS
Chains
3
Atoms
6,469
Mol. weight
103.82 kDa
Ligands
FDA
Released
29 May 2007

Explore 2UXN in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2UXN contains 41 α-helices and 34 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 33 helices, 34 β-strands

ElementResiduesLengthSheet
α-helix174-1807
α-helix190-1956
α-helix197-2015
α-helix204-22320
β-strand22711
α-helix231-2377
α-helix238-2392
α-helix246-25813
β-strand26811
α-helix272-2743
β-strand280-28452
α-helix288-30013
β-strand303-30752
β-strand319-32243
β-strand325-32843
β-strand333-33424
β-strand33815
α-helix342-3487
β-strand353-35534
α-helix356-3572
β-strand362-36326
α-helix3681
β-strand36916
α-helix370-3712
α-helix372-39423
β-strand40017
β-strand40517
α-helix4061
β-strand40718
α-helix408-46760
α-helix4691
α-helix474-51239
α-helix523-53917
β-strand54719
β-strand54818
α-helix556-5583
α-helix559-5602
β-strand56115
β-strand565-56734
α-helix573-5797
β-strand583-58532
β-strand588-596910
β-strand599-606810
β-strand613-618610
β-strand620-62342
α-helix627-6315
β-strand638-640310
α-helix642-6443
α-helix645-6539
β-strand655-656211
β-strand660-66566
β-strand677-68046
β-strand693-69536
β-strand702-70766
α-helix709-7157
α-helix720-73516
α-helix741-7433
β-strand745-74846
β-strand762-763211
β-strand76519
α-helix770-7778
β-strand78012
α-helix782-7843
α-helix789-7946
β-strand796-79832
α-helix801-8033
α-helix811-82919
Chain B: 8 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix310-3112
α-helix318-3247
α-helix330-36233
α-helix368-3703
α-helix385-39814
α-helix402-4098
α-helix414-42310
α-helix430-4389

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Lysine-specific histone demethylase 1Aprotein666HOMO SAPIENSO60341 (AlphaFold model)
Rest corepressor 1Bprotein235HOMO SAPIENSQ9UKL0 (AlphaFold model)
Histone H3.1Eprotein21HOMO SAPIENSP68431 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2UXN_1 LYSINE-SPECIFIC HISTONE DEMETHYLASE 1 (chains A)
PSGVEGAAFQSRLPHDRMTSQEAACFPDIISGPQQTQKVFLFIRNRTLQLWLDNPKIQLT
FEATLQQLEAPYNSDTVLVHRVHSYLERHGLINFGIYKRIKPLPTKKTGKVIIIGSGVSG
LAAARQLQSFGMDVTLLEARDRVGGRVATFRKGNYVADLGAMVVTGLGGNPMAVVSKQVN
MELAKIKQKCPLYEANGQAVPKEKDEMVEQEFNRLLEATSYLSHQLDFNVLNNKPVSLGQ
ALEVVIQLQEKHVKDEQIEHWKKIVKTQEELKELLNKMVNLKEKIKELHQQYKEASEVKP
PRDITAEFLVKSKHRDLTALCKEYDELAETQGKLEEKLQELEANPPSDVYLSSRDRQILD
WHFANLEFANATPLSTLSLKHWDQDDDFEFTGSHLTVRNGYSCVPVALAEGLDIKLNTAV
RQVRYTASGCEVIAVNTRSTSQTFIYKCDAVLCTLPLGVLKQQPPAVQFVPPLPEWKTSA
VQRMGFGNLNKVVLCFDRVFWDPSVNLFGHVGSTTASRGELFLFWNLYKAPILLALVAGE
AAGIMENISDDVIVGRCLAILKGIFGSSAVPQPKETVVSRWRADPWARGSYSYVAAGSSG
NDYDLMAQPITPGPSIPGAPQPIPRLFFAGEHTIRNYPATVHGALLSGLREAGRIADQFL
GAMYTL
Sequence of entity 2 (B), FASTA
>2UXN_2 REST COREPRESSOR 1 (chains B)
MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGSEFGRPTETVPQVKKEKHSTQAKNRAK
RKPPKGMFLSQEDVEAVSANATAATTVLRQLDMELVSVKRQIQNIKQTNSALKEKLDGGI
EPYRLPEVIQKCNARWTTEEQLLAVQAIRKYGRDFQAISDVIGNKSVVQVKNFFVNYRRR
FNIDEVLQEWEAEHGKEETNGPSNQKPVKSPDNSIKMPEEEDEAPVLDVRYASAS
Sequence of entity 3 (E), FASTA
>2UXN_3 HISTONE H3.1 (chains E)
ARTXQTARKSTGGKAPRKQLA

Ligands and cofactors

IDNameFormulaCopies
FDADihydroflavine-adenine dinucleotideC27 H35 N9 O15 P21

Water and common crystallization additives (GOL, CL) are not listed.

Primary citation

Structural Basis of Histone Demethylation by Lsd1 Revealed by Suicide Inactivation. Yang, M., Culhane, J.C., Szewczuk, L.M. et al. Nat Struct Mol Biol (2007) 14:535. DOI 10.1038/NSMB1255 · PubMed

Other PDB entries of the same protein (UniProt O60341 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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