1HKA
6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE
Summary for 1HKA
Entry DOI | 10.2210/pdb1hka/pdb |
Descriptor | 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE (2 entities in total) |
Functional Keywords | pyrophosphoryl transfer, pyrophosphokinase, kinase, folate, 6-hydroxymethyl-7, 8-dihydropterin, transferase |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 17966.53 |
Authors | |
Primary citation | Xiao, B.,Shi, G.,Chen, X.,Yan, H.,Ji, X. Crystal structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, a potential target for the development of novel antimicrobial agents. Structure Fold.Des., 7:489-496, 1999 Cited by PubMed Abstract: Folate cofactors are essential for life. Mammals derive folates from their diet, whereas most microorganisms must synthesize folates de novo. Enzymes of the folate pathway therefore provide ideal targets for the development of antimicrobial agents. 6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyzes the transfer of pyrophosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin (HP), the first reaction in the folate biosynthetic pathway. PubMed: 10378268DOI: 10.1016/S0969-2126(99)80065-3 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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