1.14.11.73: [protein]-arginine 3-hydroxylase

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For detailed information about [protein]-arginine 3-hydroxylase, go to the full flat file.

Reaction

Synonyms

JMJD5, KDM8

ECTree

     1 Oxidoreductases

         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen

             1.14.11 With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor

                1.14.11.73 [protein]-arginine 3-hydroxylase

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Results	in table
4	AA Sequence
2	Crystallization (Commentary)
2	General Information
1	Inhibitors
1	Metals/Ions
3	Organism
3	Protein Variants
1	Reaction
3	Reference
4	Substrates and Products (Substrate)
6	Synonyms
1	Systematic Name

Crystallization

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Crystallization on EC 1.14.11.73 - [protein]-arginine 3-hydroxylase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

structures of N-terminally truncated (aa 153-416 and aa 183-416) constructs and in complex with substrate RPS6. The JMJD5 active site contains a metal centre, which is octahedrally coordinated by an HXD..H motif, the 2-oxoglutarate oxalyl group and a water molecule, which is likely replaced by a dioxygen during catalysis

Homo sapiens

Q8N371

757771

the complex structures of JMJD5 and arginine derivatives reveals a Tudor domain-like binding pocket to accommodate the methylated sidechain of arginine, but not lysine

Mus musculus

Q9CXT6

765815