4TN7: Mouse KDM2A-H3K36ME-NO complex

Crystal structure of mouse KDM2A-H3K36ME-NO complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 13 May 2015.

Method
X-ray diffraction
Resolution
2.2 Å
Organisms
Mus musculus, Homo sapiens
Chains
6
Atoms
7,105
Mol. weight
96.82 kDa
Ligands
SIN, NO, FE
Released
13 May 2015

Explore 4TN7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4TN7 contains 42 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: 17 helices, 18 β-strands

ElementResiduesLengthSheet
α-helix40-456
β-strand5011
β-strand55-5622
α-helix59-613
α-helix64-707
β-strand76-7832
β-strand8713
α-helix95-1028
β-strand107-11262
β-strand118-12252
α-helix123-1308
β-strand141-14772
α-helix154-1563
β-strand15813
α-helix161-1666
α-helix168-1714
α-helix175-1784
β-strand18714
β-strand199-20352
β-strand208-21251
α-helix215-2173
β-strand219-22682
β-strand229-23461
α-helix238-25013
α-helix258-2614
β-strand266-27051
β-strand275-27842
α-helix2791
β-strand283-28751
β-strand292-29982
α-helix305-31713
α-helix322-3243
α-helix329-34517
β-strand35015
α-helix352-36211
Chains B and D: 4 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix455-46915
α-helix473-4764
β-strand48215
α-helix485-49814
α-helix504-5074
Chain C: 17 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-strand117-12267
α-helix123-1319
β-strand141-14777
α-helix154-1563
β-strand15818
α-helix161-1666
α-helix168-1714
α-helix175-1784
β-strand18719
β-strand199-20357
β-strand208-21256
α-helix215-2173
β-strand219-22687
β-strand229-23466
α-helix238-25013
α-helix252-2543
β-strand266-27056
β-strand275-27847
α-helix2791
β-strand283-28756
β-strand292-29987
α-helix305-31713
α-helix322-3243
α-helix329-34517
β-strand350110
α-helix352-36211
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)
PeptideE, Fprotein15Homo sapiensP68431 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>4TN7_1 Lysine-specific demethylase 2A (chains A, C)
RTFDLEEKLQTNKYNANFVTFMEGKDFNVEYIQRGGLRDPLIFKNSDGLGIKMPDPDFTV
NDVKMCVGSRRMVDVMDVNTQKGIEMTMAQWTRYYETPEEEREKLYNVISLEFSHTRLEN
MVQRPSTVDFIDWVDNMWPRHLKESQTESTNAILEMQYPKVQKYCLMSVRGCYTDFHVDF
GGTSVWYHIHQGGKVFWLIPPTAHNLELYENWLLSGKQGDIFLGDRVSDCQRIELKQGYT
FVIPSGWIHAVYTPTDTLVFGGNFLHSFNIPMQLKIYSIEDRTRVPNKFRYPFYYEMCWY
VLERYVYCITNRSHLTKDFQKESLSMDME
Sequence of entity 2 (B, D), FASTA
>4TN7_2 Lysine-specific demethylase 2A (chains B, D)
QVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEELASSDPKLALT
GVPIVQWP
Sequence of entity 3 (E, F), FASTA
>4TN7_3 Peptide (chains E, F)
APATGGVKKPHRYRP

Ligands and cofactors

IDNameFormulaCopies
SINSuccinic acidC4 H6 O42
NONitric oxideN O1
FEFE (III) ionFe2

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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