2WWU: Crystal structure of the catalytic domain of PHD finger protein 8

Citation:
Abstract
Crystallographic analysis of the catalytic domain of PHD finger protein 8 (PHF8), an N(epsilon)-methyl lysine histone demethylase associated with mental retardation and cleft lip/palate, reveals a double-stranded beta-helix fold with conserved Fe(II) and cosubstrate binding sites typical of the 2-oxoglutarate dependent oxygenases. The PHF8 active site is highly conserved with those of the FBXL10/11demethylases, which are also selective for the di-/mono-methylated lysine states, but differs from that of the JMJD2 demethylases which are selective for tri-/di-methylated states. The results rationalize the lack of activity for the clinically observed F279S PHF8 variant and they will help to identify inhibitors selective for specific N(epsilon)-methyl lysine demethylase subfamilies.
PDB ID: 2WWUDownload
MMDB ID: 78136
PDB Deposition Date: 2009/10/29
Updated in MMDB: 2012/12
Experimental Method:
x-ray diffraction
Resolution: 2.15  Å
Source Organism:
Similar Structures:
Biological Unit for 2WWU: dimeric; determined by author and by software (PISA)
Molecular Components in 2WWU
Label Count Molecule
Proteins (2 molecules)
2
PHD Finger Protein 8(Gene symbol: PHF8)
Molecule annotation
Chemicals (29 molecules)
1
13
2
10
3
2
4
4
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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