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 | 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 | Comment | Organism | Structure |
---|---|---|---|
Fe3+ | - |
Mycobacterium tuberculosis | |
Mn2+ | - |
Mycobacterium tuberculosis |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mycobacterium tuberculosis | P9WP65 | product of Rv0805 gene | - |
Mycobacterium tuberculosis H37Rv | P9WP65 | product of Rv0805 gene | - |
Subunits | Comment | Organism |
---|---|---|
dimer | crystallization data | Mycobacterium tuberculosis |