User:John Hangasky/Sandbox 1
From Proteopedia
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1h2l, resolution 2.25Å () | |||||||||
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Ligands: | , , | ||||||||
Related: | 1d7g, 1h2k, 1h2m, 1h2n, 1l8c, 1lm8, 1lqb | ||||||||
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Resources: | FirstGlance, OCA, RCSB, PDBsum | ||||||||
Coordinates: | save as pdb, mmCIF, xml |
Factor Inhibiting HIF
Hypoxia Inducible Factor (HIF)is a transcription activator that regulates over 100 genes, many of which are important for development. HIF has been found to be over expressed in many cancers. Factor Inhibing HIF (FIH) is a non-heme Iron (II) α-ketoglutarate dependent asparaginyl hydroxylase that regulates HIF. In normoxic conditions (high oxygen concenrations), molecular oxygen is used to hydroxylate HIF, preventing HIF from binding to p300, a transcription coactivator. However, in hypoxic conditions (low oxygen concentrations), this hydroxylation does not occur.
FIH binds to the C-terminal activation domain (CTAD) of HIF. This binding domain, , colored teal.
Active Site
The contains an iron II core. The iron core is coordinated by 2 histidine residues, an asparagine residue, α-ketoglutarate and one water molecule. α-ketoglutarate chelates in a bidentate manner, making the coordination number of the iron 6. In the depiction of the Histidines are colored blue, Aspartate is colored red, Iron is the white sphere, and α-KG is colored yellow. The sixth coordination site is usually occupied by water, not shown here.
Enzyme Surface
In this depiction, the of FIH is seen.