Crystallization (Comment) | Organism |
---|---|
comparison of structural models of the GDP-mannose diphosphorylases from human and Leishmania donovani. Residues Leu14, Val15, Ala60, Leu92 and Pro97 surround the hydrophobic bicycle of the nucleotide, while the amine groups of the latter interact with Glu88. The ribose ring belonging to the substrate is bound to protein residues Asn116 and Ser117. The magnesium ion is chelated by Asp118 and Asp226, and the diphosphate group makes electrostatic interactions with residues Arg21 and Lys31, which belong to the GGXGXRLXPLX5PK diphosphorylase signature | Leishmania donovani |
comparison of structural models of the GDP-mannose diphosphorylases from human and Leishmania donovani. The human active site is site very similar to the Leishmania donovani one. Leishmania donovani GDP-mannose diphosphorylase makes more interactions with its substrate than the human enzyme does | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | Q9Y5P6 | - |
- |
Leishmania donovani | E9BG32 | - |
- |
Leishmania donovani BPK282A1 | E9BG32 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
GMPPB | - |
Homo sapiens |
LDBPK_230120 | - |
Leishmania donovani |