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1HKA

6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE

Summary for 1HKA
Entry DOI10.2210/pdb1hka/pdb
Descriptor6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE (2 entities in total)
Functional Keywordspyrophosphoryl transfer, pyrophosphokinase, kinase, folate, 6-hydroxymethyl-7, 8-dihydropterin, transferase
Biological sourceEscherichia coli
Total number of polymer chains1
Total formula weight17966.53
Authors
Xiao, B.,Shi, G.,Chen, X.,Yan, H.,Ji, X. (deposition date: 1998-09-29, release date: 1999-06-08, Last modification date: 2023-08-30)
Primary citationXiao, 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: 10378268
DOI: 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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