4AI9: Jmjd2a Complexed With Daminozide

Citation:
Abstract
The JmjC oxygenases catalyze the N-demethylation of N(epsilon)-methyl lysine residues in histones and are current therapeutic targets. A set of human 2-oxoglutarate analogues were screened using a unified assay platform for JmjC demethylases and related oxygenases. Results led to the finding that daminozide (N-(dimethylamino)succinamic acid, 160 Da), a plant growth regulator, selectively inhibits the KDM2/7 JmjC subfamily. Kinetic and crystallographic studies reveal that daminozide chelates the active site metal via its hydrazide carbonyl and dimethylamino groups.
PDB ID: 4AI9Download
MMDB ID: 103492
PDB Deposition Date: 2012/2/8
Updated in MMDB: 2012/10
Experimental Method:
x-ray diffraction
Resolution: 2.25  Å
Source Organism:
Similar Structures:
Biological Unit for 4AI9: monomeric; determined by author and by software (PISA)
Molecular Components in 4AI9
Label Count Molecule
Protein (1 molecule)
1
Lysine-specific Demethylase 4A(Gene symbol: KDM4A)
Molecule annotation
Chemicals (5 molecules)
1
1
2
1
3
1
4
2
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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