3.9.1.2: protein arginine phosphatase

This is an abbreviated version!
For detailed information about protein arginine phosphatase, go to the full flat file.

Reaction

Synonyms

YwlE

ECTree

3 Hydrolases

3.9 Acting on phosphorus-nitrogen bonds

3.9.1 Acting on phosphorus-nitrogen bonds (only sub-subclass identified to date)

3.9.1.2 protein arginine phosphatase

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Results	in table
53	AA Sequence
2	Application
2	Cloned(Commentary)
1	Crystallization (Commentary)
5	General Information
1	Inhibitors
2	kcat/KM [mM/s]
10	KM Value [mM]
1	Localization
4	Natural Substrates/ Products (Substrates)
20	Organism
9	Protein Variants
1	Purification (Commentary)
1	Reaction
10	Reference
1	Source Tissue
19	Substrates and Products (Substrate)
4	Synonyms
1	Systematic Name
2	Turnover Number [1/s]

Crystallization

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of the Enzyme Summary Page.

Crystallization on EC 3.9.1.2 - protein arginine phosphatase

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in complex with phosphate.The phosphate-binding site is formed by the side chain of Arg13, the backbone amides of the phosphate-loop and the positive end of the macrodipole of helix H1, which together generate a highly positively charged pocket at the bottom of the substrate-binding cleft. The substrate-mimicking Arg149 is sandwiched between Thr11, Asp118, and Phe120 with its guanidinium group hydrogen bonding to Asp118. Structure of mutant C7S in complex with phosphate shows the formation of a covalent phospho-Ser7 adduct indicating that the crystallized mutant mimics the phospho-enzyme intermediate of the dephosphorylation reaction

Geobacillus stearothermophilus

S0F332

729550