Histone demethylase KDM2A-H3K36ME1-alpha-KG complex structure. Determined by X-ray diffraction at 2.1 Å resolution. Released 5 Nov 2014.
Explore 4QWN in 3D Show helices and sheets RCSB PDB PDBe
4QWN contains 44 α-helices and 41 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 40-45 | 6 | |
| β-strand | 50 | 1 | 1 |
| α-helix | 54 | 1 | |
| β-strand | 55-56 | 2 | 2 |
| α-helix | 59-61 | 3 | |
| α-helix | 64-70 | 7 | |
| β-strand | 76-78 | 3 | 2 |
| β-strand | 87 | 1 | 3 |
| α-helix | 95-102 | 8 | |
| β-strand | 107-112 | 6 | 2 |
| β-strand | 117-122 | 6 | 2 |
| α-helix | 123-131 | 9 | |
| β-strand | 141-147 | 7 | 2 |
| α-helix | 152-156 | 5 | |
| β-strand | 158 | 1 | 3 |
| α-helix | 161-166 | 6 | |
| α-helix | 168-172 | 5 | |
| α-helix | 175-180 | 6 | |
| β-strand | 187 | 1 | 4 |
| α-helix | 188-190 | 3 | |
| β-strand | 199-203 | 5 | 2 |
| β-strand | 208-212 | 5 | 1 |
| α-helix | 215-217 | 3 | |
| β-strand | 219-226 | 8 | 2 |
| β-strand | 229-234 | 6 | 1 |
| α-helix | 238-250 | 13 | |
| α-helix | 258-260 | 3 | |
| β-strand | 266-270 | 5 | 1 |
| β-strand | 275-278 | 4 | 2 |
| α-helix | 279 | 1 | |
| β-strand | 283-287 | 5 | 1 |
| β-strand | 292-299 | 8 | 2 |
| α-helix | 305-317 | 13 | |
| α-helix | 322-324 | 3 | |
| α-helix | 329-345 | 17 | |
| β-strand | 350 | 1 | 5 |
| α-helix | 352-362 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 455-469 | 15 | |
| α-helix | 473-476 | 4 | |
| β-strand | 482 | 1 | 5 |
| α-helix | 485-500 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 40-45 | 6 | |
| β-strand | 50 | 1 | 6 |
| α-helix | 54 | 1 | |
| β-strand | 55-56 | 2 | 7 |
| α-helix | 59-61 | 3 | |
| α-helix | 64-70 | 7 | |
| β-strand | 76-78 | 3 | 7 |
| β-strand | 87 | 1 | 8 |
| α-helix | 95-102 | 8 | |
| β-strand | 107-110 | 4 | 9 |
| β-strand | 111-112 | 2 | 7 |
| α-helix | 113-115 | 3 | |
| β-strand | 119-122 | 4 | 9 |
| α-helix | 123-131 | 9 | |
| β-strand | 141-147 | 7 | 7 |
| α-helix | 154-156 | 3 | |
| β-strand | 158 | 1 | 8 |
| α-helix | 161-166 | 6 | |
| α-helix | 168-172 | 5 | |
| α-helix | 175-180 | 6 | |
| β-strand | 187 | 1 | 10 |
| α-helix | 188-190 | 3 | |
| β-strand | 199-203 | 5 | 7 |
| β-strand | 208-212 | 5 | 6 |
| α-helix | 215-217 | 3 | |
| β-strand | 219-226 | 8 | 7 |
| β-strand | 229-234 | 6 | 6 |
| α-helix | 238-249 | 12 | |
| α-helix | 258-261 | 4 | |
| β-strand | 266-270 | 5 | 6 |
| β-strand | 275-278 | 4 | 7 |
| β-strand | 283-287 | 5 | 6 |
| β-strand | 292-299 | 8 | 7 |
| α-helix | 305-317 | 13 | |
| α-helix | 322-324 | 3 | |
| α-helix | 329-345 | 17 | |
| β-strand | 350 | 1 | 11 |
| α-helix | 352-363 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 455-469 | 15 | |
| α-helix | 473-475 | 3 | |
| β-strand | 482 | 1 | 11 |
| α-helix | 485-500 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 32 | 1 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lysine-specific demethylase 2A | A, C | protein | 329 | Mus musculus | P59997 (AlphaFold model) |
| Lysine-specific demethylase 2A | B, D | protein | 68 | Mus musculus | P59997 (AlphaFold model) |
| Histone H3.2 | E, F | protein | 15 | Mus musculus | P84228 (AlphaFold model) |
>4QWN_1 Lysine-specific demethylase 2A (chains A, C) RTFDLEEKLQTNKYNANFVTFMEGKDFNVEYIQRGGLRDPLIFKNSDGLGIKMPDPDFTV NDVKMCVGSRRMVDVMDVNTQKGIEMTMAQWTRYYETPEEEREKLYNVISLEFSHTRLEN MVQRPSTVDFIDWVDNMWPRHLKESQTESTNAILEMQYPKVQKYCLMSVRGCYTDFHVDF GGTSVWYHIHQGGKVFWLIPPTAHNLELYENWLLSGKQGDIFLGDRVSDCQRIELKQGYT FVIPSGWIHAVYTPTDTLVFGGNFLHSFNIPMQLKIYSIEDRTRVPNKFRYPFYYEMCWY VLERYVYCITNRSHLTKDFQKESLSMDME
>4QWN_2 Lysine-specific demethylase 2A (chains B, D) QVHLTHFELEGLRCLVDKLESLPLHKKCVPTGIEDEDALIADVKILLEELASSDPKLALT GVPIVQWP
>4QWN_3 Histone H3.2 (chains E, F) APATGGVKKPHRYRP
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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