Crystallization (Comment) | Organism |
---|---|
vapour diffusion method, hanging drops from solution: 10 mg/ml purified apo-enzyme in 10 mM MES, pH 6.0, 1 mM dithiothreitol, 5 mM MgCl2, 4°C, reservoir solution: 7-11% polyethylene glycol 5000 monomethyl ether, 0.2 M ammonium acetate, 0.1 M sodium citrate, pH 4.9, 10 mM MgCl2, 1.2-1.6 M ammonium sulfate, for AMP- or adenine-bound crystals addition of 10 mM AMP or 5 mM adenine in the reservoir solution, structure analysis | Leishmania donovani |
Protein Variants | Comment | Organism |
---|---|---|
additional information | alignment of amino acid sequences, correlation between human clinical missense mutations and structure, structure taken from Leishmania donovani enzyme | Leishmania donovani |
additional information | alignment of amino acid sequences, correlation between human clinical missense mutations and structure, structure taken from Leishmania donovani enzyme | Homo sapiens |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Leishmania donovani | |
Mg2+ | Mg2+ ligand binding site | Leishmania donovani |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P07741 | - |
- |
Leishmania donovani | Q27679 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
AMP + diphosphate = adenine + 5-phospho-alpha-D-ribose 1-diphosphate | active site structure | Leishmania donovani |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
adenine + 5-phospho-alpha-D-ribose 1-diphosphate | substrate binding structure | Leishmania donovani | AMP + diphosphate | AMP is bound in the low energy anti conformation with the ribose in the 2' endo conformation | ? |
Subunits | Comment | Organism |
---|---|---|
dimer | - |
Leishmania donovani |
More | three-dimensional structure, apo-enzyme in complexes with AMP, adenine, sulfate, citrate, subunit model | Leishmania donovani |