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PDBe Entry: 1tmj 
Crystal structure of E.coli apo-HPPK(W89A) at 1.45 Angstrom resolution
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TRANSFERASE
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X-RAY DIFFRACTION
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Resolution: 1.45 Å, R-factor: 13.1%, Free R-factor: 17.4%, Spacegroup: P 1 21 1
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21/06/2005, deposition: 10/06/2004, last revision: 24/02/2009
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Blaszczyk, J. ; Ji, X.
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Is the Critical Role of Loop 3 of Escherichia coli 6-Hydroxymethyl-7,8-dihydropterin Pyrophosphokinase in Catalysis Due to Loop-3 Residues Arginine-84 and Tryptophan-89? Site-Directed Mutagenesis, Biochemical, and Crystallographic Studies. BIOCHEMISTRY vol:44, pag:8590-8599 (2005) [PubMed ID 15952765 ]
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PYROPHOSPHOKINASE , PYROPHOSPHORYL TRANSFER , FOLATE , HPPK , 6-HYDROXYMETHYLPTERIN , 6-HYDROXYMETHYL-7 , 8-DIHYDROPTERIN , ANTIMICROBIAL AGENT , DRUG DESIGN , X-RAY CRYSTALLOGRAPHY , POINT MUTANT , STRUCTURAL MUTAGENESIS , 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, 1q0n, 1ex8, 1cbk, 1dy3, 1f9y, 1f9h, 1g4c, 1hq2, 1im6, 1kbr, 1ru2, 1ru1, 1rtz, 1rb0, 1tmm
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| A |
2-amino-4-hydroxy-6-hydroxymethyldihydropteridine 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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