4QX7: Histone demethylase kdm2a-h3k36me2 with alpha-kg

Crystal structure of histone demethylase kdm2a-h3k36me2 with alpha-kg. Determined by X-ray diffraction at 2.34 Å resolution. Released 5 Nov 2014.

Method
X-ray diffraction
Resolution
2.34 Å
Organism
Mus musculus
Chains
6
Atoms
7,027
Mol. weight
96.88 kDa
Ligands
NI, AKG
Released
5 Nov 2014

Explore 4QX7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4QX7 contains 43 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: 18 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-strand117-12262
α-helix123-1319
α-helix134-1363
β-strand141-14772
α-helix152-1565
β-strand15813
α-helix161-1666
α-helix168-1725
α-helix175-1806
β-strand18714
β-strand199-20352
β-strand207-21261
α-helix215-2173
β-strand219-22682
β-strand229-23461
α-helix238-25013
α-helix258-2603
β-strand266-27051
β-strand275-27842
β-strand283-28861
β-strand292-29982
α-helix305-31814
α-helix322-3243
α-helix329-34517
β-strand35015
α-helix352-36312
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
α-helix541
β-strand55-5627
α-helix59-613
α-helix64-707
β-strand76-7837
β-strand8718
α-helix95-1028
β-strand107-11267
β-strand117-12267
α-helix123-1319
α-helix134-1363
β-strand141-14777
α-helix152-1565
β-strand15818
α-helix161-1666
α-helix168-1725
α-helix175-1806
β-strand18719
α-helix188-1903
β-strand199-20357
β-strand207-21266
α-helix215-2173
β-strand219-22687
β-strand229-23466
α-helix238-25013
α-helix258-2603
β-strand266-27056
β-strand275-27847
β-strand283-28866
β-strand292-29987
α-helix305-31814
α-helix322-3243
α-helix329-34517
β-strand350110
α-helix352-36312
Chain D: 3 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix455-46915
α-helix473-4753
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
>4QX7_1 Lysine-specific demethylase 2A (chains A, C)
RTFDLEEKLQTNKYNANFVTFMEGKDFNVEYIQRGGLRDPLIFKNSDGLGIKMPDPDFTV
NDVKMCVGSRRMVDVMDVNTQKGIEMTMAQWTRYYETPEEEREKLYNVISLEFSHTRLEN
MVQRPSTVDFIDWVDNMWPRHLKESQTESTNAILEMQYPKVQKYCLMSVRGCYTDFHVDF
GGTSVWYHIHQGGKVFWLIPPTAHNLELYENWLLSGKQGDIFLGDRVSDCQRIELKQGYT
FVIPSGWIHAVYTPTDTLVFGGNFLHSFNIPMQLKIYSIEDRTRVPNKFRYPFYYEMCWY
VLERYVYCITNRSHLTKDFQKESLSMDME
Sequence of entity 2 (B, D), FASTA
>4QX7_2 Lysine-specific demethylase 2A (chains B, D)
QVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEELASSDPKLALT
GVPIVQWP
Sequence of entity 3 (E, F), FASTA
>4QX7_3 Histone H3.2 (chains E, F)
APATGGVKKPHRYRP

Ligands and cofactors

IDNameFormulaCopies
NINickel (II) ionNi2
AKG2-oxoglutaric acidC5 H6 O52

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:

Browse structure collections

About this viewer

MolViewer shows 4QX7 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.