Literature summary for 3.1.4.17 extracted from

Shenoy, A.R.; Capuder, M.; Draskovic, P.; Lamba, D.; Visweswariah, S.S.; Podobnik, M.
Structural and biochemical analysis of the Rv0805 cyclic nucleotide phosphodiesterase from Mycobacterium tuberculosis (2007), J. Mol. Biol., 365, 211-225.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
enzyme is a Fe3+-Mn2+-binuclear dimer, and the metal ions contribute to dimerization. Wild-type has a molecule of phosphate bound in the active site. Structure of mutants N97A lacking one of the Mn2+ coordinating residues and D66A that has a compromised cAMP hydrolytic activity	Mycobacterium tuberculosis

Protein Variants

Protein Variants	Comment	Organism
D66A	compromised cAMP hydrolytic activity, crystallization data	Mycobacterium tuberculosis
N97A	almost complete loss of activity, lacks one of the Mn2+ coordinating residues	Mycobacterium tuberculosis

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe3+	-	Mycobacterium tuberculosis
Mn2+	-	Mycobacterium tuberculosis

Organism

Organism	UniProt	Comment	Textmining
Mycobacterium tuberculosis	P9WP65	product of Rv0805 gene	-
Mycobacterium tuberculosis H37Rv	P9WP65	product of Rv0805 gene	-

Subunits

Subunits	Comment	Organism
dimer	crystallization data	Mycobacterium tuberculosis

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Release 2023.1 (January 2023)