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PDBe Entry: 1f9h 
CRYSTAL STRUCTURE OF THE TERNARY COMPLEX OF E. COLI HPPK(R92A) WITH MGAMPCPP AND 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN AT 1.50 ANGSTROM RESOLUTION
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TRANSFERASE
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X-RAY DIFFRACTION
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Resolution: 1.5 Å, R-factor: 8.36%, Free R-factor: 15.13%, Spacegroup: C 1 2 1
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15/04/2003, deposition: 10/07/2000, last revision: 24/02/2009
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Blaszczyk, J. ; Ji, X.
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Dynamic Roles of Arginine Residues 82 and 92 of Escherichia coli
6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase: Crystallographic
Studies BIOCHEMISTRY vol:42, pag:1573-1580 (2003) [PubMed ID 12578370 ]
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PYROPHOSPHOKINASE , PYROPHOSPHORYL TRANSFER , CATALYTIC MECHANISM , FOLATE , HPPK , PTERIN , 6-HYDROXYMETHYL-7 , 8-DIHYDROPTERIN , TERNARY COMPLEX , SUBSTRATE SPECIFICITY , ANTIMICROBIAL AGENT , DRUG DESIGN , X-RAY CRYSTALLOGRAPHY , TRANSFERASE
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2.7.6.3 ExPASy BRENDA (A)
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Escherichia coli 562 (A)
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2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase (EC 2.7.6.3) (7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase) (HPPK) (6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase) (PPPK) P26281 (A)
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A
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1hka, 1eqm, 1eq0, 1eqo, 1ex8, 1cbk, 1dy3
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| A |
6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE |
Protein |
P26281 (HPPK_ECOLI)
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158 |
100% |
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| A |
MAGNESIUM ION |
MG
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| A |
CHLORIDE ION |
CL
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| A |
DIPHOSPHOMETHYLPHOSPHONIC ACID ADENOSYL ESTER |
APC
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| A |
2-AMINO-6-HYDROXYMETHYL-7,8-DIHYDRO-3H-PTERIDIN-4-ONE |
PH2
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