4QXC: Histone demethylase KDM2A-H3K36ME2 with NOG

Crystal structure of histone demethylase KDM2A-H3K36ME2 with NOG. Determined by X-ray diffraction at 1.75 Å resolution. Released 5 Nov 2014.

Method
X-ray diffraction
Resolution
1.75 Å
Organism
Mus musculus
Chains
6
Atoms
7,200
Mol. weight
96.88 kDa
Ligands
OGA, NI
Released
5 Nov 2014

Explore 4QXC in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4QXC contains 45 α-helices and 40 β-strands across 6 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: 20 helices, 18 β-strands

ElementResiduesLengthSheet
α-helix40-456
β-strand5011
α-helix541
β-strand55-5622
α-helix59-613
α-helix64-707
β-strand76-7832
β-strand8713
α-helix95-1028
β-strand107-11262
β-strand118-12252
α-helix123-1319
α-helix134-1363
β-strand141-14772
α-helix154-1563
β-strand15813
α-helix161-1666
α-helix168-1714
α-helix175-1806
β-strand18714
α-helix188-1903
β-strand199-20352
β-strand208-21251
α-helix215-2173
β-strand219-22682
β-strand229-23461
α-helix238-25013
α-helix258-2603
β-strand266-27051
α-helix2711
β-strand275-27842
β-strand283-28751
β-strand292-29982
α-helix305-31713
α-helix322-3243
α-helix329-34517
β-strand35015
α-helix352-36211
Chain B: 3 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix455-46915
α-helix473-4764
β-strand48215
α-helix485-49915
Chain C: 19 helices, 18 β-strands
ElementResiduesLengthSheet
α-helix40-456
β-strand5016
β-strand55-5627
α-helix59-613
α-helix64-707
β-strand76-7837
β-strand8718
α-helix95-1028
β-strand107-11267
β-strand118-12257
α-helix123-1308
α-helix134-1363
β-strand141-14777
α-helix154-1563
β-strand15818
α-helix161-1666
α-helix168-1725
α-helix175-1806
β-strand18719
α-helix188-1903
β-strand199-20357
β-strand208-21256
α-helix215-2173
β-strand219-22687
β-strand228-23476
α-helix238-25013
α-helix252-2543
α-helix258-2603
β-strand266-27166
β-strand275-27847
β-strand283-28756
β-strand292-29987
α-helix305-31713
α-helix322-3243
α-helix329-34517
β-strand350110
α-helix352-36211
Chain D: 3 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix455-47016
α-helix473-4764
β-strand482110
α-helix485-49915
Chains E and F: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand3214

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Lysine-specific demethylase 2AA, Cprotein329Mus musculusP59997 (AlphaFold model)
Lysine-specific demethylase 2AB, Dprotein68Mus musculusP59997 (AlphaFold model)
Histone H3.2E, Fprotein15Mus musculusP84228 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>4QXC_1 Lysine-specific demethylase 2A (chains A, C)
RTFDLEEKLQTNKYNANFVTFMEGKDFNVEYIQRGGLRDPLIFKNSDGLGIKMPDPDFTV
NDVKMCVGSRRMVDVMDVNTQKGIEMTMAQWTRYYETPEEEREKLYNVISLEFSHTRLEN
MVQRPSTVDFIDWVDNMWPRHLKESQTESTNAILEMQYPKVQKYCLMSVRGCYTDFHVDF
GGTSVWYHIHQGGKVFWLIPPTAHNLELYENWLLSGKQGDIFLGDRVSDCQRIELKQGYT
FVIPSGWIHAVYTPTDTLVFGGNFLHSFNIPMQLKIYSIEDRTRVPNKFRYPFYYEMCWY
VLERYVYCITNRSHLTKDFQKESLSMDME
Sequence of entity 2 (B, D), FASTA
>4QXC_2 Lysine-specific demethylase 2A (chains B, D)
QVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEELASSDPKLALT
GVPIVQWP
Sequence of entity 3 (E, F), FASTA
>4QXC_3 Histone H3.2 (chains E, F)
APATGGVKKPHRYRP

Ligands and cofactors

IDNameFormulaCopies
OGAN-oxalylglycineC4 H5 N O52
NINickel (II) ionNi2

Primary citation

A molecular threading mechanism underlies Jumonji lysine demethylase KDM2A regulation of methylated H3K36. Cheng, Z., Cheung, P., Kuo, A.J. et al. Genes Dev (2014) 28:1758-1771. DOI 10.1101/gad.246561.114 · PubMed

Other PDB entries of the same protein (UniProt P59997 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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