9GLE: Lysine-specific demethylase 4A

Jumonji domain-containing protein 2A with crystallization epitope mutations A91T:T93S. Determined by X-ray diffraction at 1.88 Å resolution. Released 18 Sept 2024.

Method
X-ray diffraction
Resolution
1.88 Å
Organism
Homo sapiens
Chains
2
Atoms
6,084
Mol. weight
84.84 kDa
Ligands
ZN, NI
Released
18 Sept 2024

Explore 9GLE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9GLE contains 47 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: 22 helices, 17 β-strands

ElementResiduesLengthSheet
α-helix14-152
β-strand16-1831
α-helix22-254
α-helix28-3710
α-helix40-434
β-strand45-4841
β-strand67-6822
β-strand72-7983
β-strand82-8983
β-strand93-9422
α-helix95-1039
α-helix109-1113
α-helix115-12511
β-strand132-13323
β-strand134-13851
α-helix157-1604
β-strand176-18051
β-strand185-18954
α-helix192-1943
β-strand196-20491
β-strand207-21264
α-helix214-2163
α-helix217-22711
α-helix229-2346
α-helix238-2414
β-strand244-24633
α-helix248-2536
β-strand259-26354
α-helix2641
β-strand268-27141
β-strand276-28164
β-strand285-29281
α-helix297-3037
α-helix304-3074
α-helix319-3257
α-helix327-3293
α-helix330-3345
α-helix347-3482
α-helix349-3546
Chain B: 25 helices, 17 β-strands
ElementResiduesLengthSheet
α-helix14-163
β-strand17-1825
α-helix22-254
α-helix28-3710
α-helix40-434
β-strand45-4845
α-helix49-513
α-helix63-653
β-strand67-6826
β-strand72-7987
β-strand82-8987
β-strand93-9426
α-helix95-1039
α-helix109-1113
α-helix115-12511
α-helix130-1312
β-strand132-13327
β-strand134-13855
α-helix157-1615
β-strand176-18055
β-strand185-18958
α-helix192-1943
β-strand196-20495
β-strand207-21268
α-helix214-2163
α-helix217-22711
α-helix229-2346
α-helix238-2414
β-strand244-24637
α-helix248-2536
β-strand259-26358
α-helix2641
β-strand268-27145
β-strand276-28168
β-strand285-29285
α-helix297-3037
α-helix304-3074
α-helix319-3257
α-helix327-3293
α-helix330-3345
α-helix347-3482
α-helix349-3546

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Lysine-specific demethylase 4AA, Bprotein360Homo sapiensO75164 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>9GLE_1 Lysine-specific demethylase 4A (chains A, B)
SMASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRASY
DDIDDLVIPAPIQQLVTGQSGLFTQYNIQKKTMSVREFRKIANSDKYCTPRYSEFEELER
KYWKNLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNTPYLYFG
MWKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLR
HKMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEY
GKQAVLCSCRKDMVKISMDVFVRKFQPERYKLWKAGKDNTVIDHTLPTPEAAEFLKESEL

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2
NINickel (II) ionNi2

Water and common crystallization additives (EDO, SO4) are not listed.

Primary citation

A fast, parallel method for efficiently exploring crystallization behaviour of large numbers of protein variants. Fairhead, M., Strain-Damerell, C., Ye, M. et al. To be published.

Other PDB entries of the same protein (UniProt O75164 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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