Crystal Structure of KDM4A with compound YP-03-038. Determined by X-ray diffraction at 1.83 Å resolution. Released 10 Apr 2019.
Explore 6G5W in 3D Show helices and sheets RCSB PDB PDBe
6G5W 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 5-7 | 3 | |
| α-helix | 13-15 | 3 | |
| β-strand | 16-17 | 2 | 1 |
| α-helix | 21-24 | 4 | |
| α-helix | 27-36 | 10 | |
| α-helix | 39-42 | 4 | |
| β-strand | 44-47 | 4 | 1 |
| α-helix | 48-50 | 3 | |
| β-strand | 66-67 | 2 | 2 |
| β-strand | 71-78 | 8 | 3 |
| β-strand | 81-88 | 8 | 3 |
| β-strand | 92-93 | 2 | 2 |
| α-helix | 94-102 | 9 | |
| α-helix | 108-110 | 3 | |
| α-helix | 114-124 | 11 | |
| β-strand | 131-132 | 2 | 3 |
| β-strand | 133-137 | 5 | 1 |
| α-helix | 158-164 | 7 | |
| β-strand | 175-179 | 5 | 1 |
| β-strand | 184-188 | 5 | 4 |
| α-helix | 189-190 | 2 | |
| α-helix | 191-193 | 3 | |
| β-strand | 195-203 | 9 | 1 |
| β-strand | 206-211 | 6 | 4 |
| α-helix | 213-215 | 3 | |
| α-helix | 216-226 | 11 | |
| α-helix | 228-233 | 6 | |
| α-helix | 237-240 | 4 | |
| β-strand | 243-245 | 3 | 3 |
| α-helix | 247-252 | 6 | |
| β-strand | 258-262 | 5 | 4 |
| β-strand | 267-270 | 4 | 1 |
| β-strand | 275-280 | 6 | 4 |
| β-strand | 284-291 | 8 | 1 |
| α-helix | 296-302 | 7 | |
| α-helix | 303-306 | 4 | |
| α-helix | 318-324 | 7 | |
| α-helix | 329-333 | 5 | |
| α-helix | 345-347 | 3 | |
| α-helix | 348-351 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 13-15 | 3 | |
| β-strand | 16-17 | 2 | 5 |
| α-helix | 21-25 | 5 | |
| α-helix | 27-36 | 10 | |
| α-helix | 39-42 | 4 | |
| β-strand | 44-47 | 4 | 5 |
| α-helix | 48-50 | 3 | |
| β-strand | 66-67 | 2 | 6 |
| β-strand | 71-78 | 8 | 7 |
| β-strand | 81-88 | 8 | 7 |
| α-helix | 89-91 | 3 | |
| β-strand | 92-93 | 2 | 6 |
| α-helix | 94-102 | 9 | |
| α-helix | 108-110 | 3 | |
| α-helix | 114-124 | 11 | |
| β-strand | 131-132 | 2 | 7 |
| β-strand | 133-137 | 5 | 5 |
| α-helix | 156-158 | 3 | |
| α-helix | 159-162 | 4 | |
| β-strand | 175-179 | 5 | 5 |
| β-strand | 184-188 | 5 | 8 |
| α-helix | 189-190 | 2 | |
| α-helix | 191-193 | 3 | |
| β-strand | 195-203 | 9 | 5 |
| β-strand | 206-211 | 6 | 8 |
| α-helix | 213-215 | 3 | |
| α-helix | 216-226 | 11 | |
| α-helix | 228-233 | 6 | |
| α-helix | 237-240 | 4 | |
| β-strand | 243-245 | 3 | 7 |
| α-helix | 247-252 | 6 | |
| β-strand | 258-262 | 5 | 8 |
| α-helix | 263 | 1 | |
| β-strand | 267-270 | 4 | 5 |
| β-strand | 275-280 | 6 | 8 |
| β-strand | 284-291 | 8 | 5 |
| α-helix | 296-302 | 7 | |
| α-helix | 318-324 | 7 | |
| α-helix | 326-333 | 8 | |
| α-helix | 346-347 | 2 | |
| α-helix | 348-350 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lysine-specific demethylase 4A | A, B | protein | 359 | Homo sapiens | O75164 (AlphaFold model) |
>6G5W_1 Lysine-specific demethylase 4A (chains A, B) MASESETLNPSARIMTFYPTMEEFRNFSRYIAYIESQGAHRAGLAKVVPPKEWKPRASYD DIDDLVIPAPIQQLVTGQSGLFTQYNIQKKAMTVREFRKIANSDKYCTPRYSEFEELERK YWKNLTFNPPIYGADVNGTLYEKHVDEWNIGRLRTILDLVEKESGITIEGVNTPYLYFGM WKTSFAWHTEDMDLYSINYLHFGEPKSWYSVPPEHGKRLERLAKGFFPGSAQSCEAFLRH KMTLISPLMLKKYGIPFDKVTQEAGEFMITFPYGYHAGFNHGFNCAESTNFATRRWIEYG KQAVLCSCRKDMVKISMDVFVRKFQPERYKLWKAGKDNTVIDHTLPTPEAAEFLKESEL
| ID | Name | Formula | Copies |
|---|---|---|---|
| ENZ | (4~{R})-5-methyl-4-phenyl-2-pyridin-2-yl-pyrazolidin-3-one | C15 H15 N3 O | 1 |
| CIT | Citric acid | C6 H8 O7 | 3 |
| NI | Nickel (II) ion | Ni | 4 |
| ZN | Zinc ion | Zn | 2 |
Water and common crystallization additives (NA, EDO) are not listed.
Enhanced Properties of a Benzimidazole Benzylpyrazole Lysine Demethylase Inhibitor: Mechanism-of-Action, Binding Site Analysis, and Activity in Cellular Models of Prostate Cancer. Carter, D.M., Specker, E., Malecki, P.H. et al. J Med Chem (2021) 64:14266-14282. DOI 10.1021/acs.jmedchem.1c00693 · PubMed
Other PDB entries of the same protein (UniProt O75164 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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