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PDBe Entry: 1tmj view

Crystal structure of E.coli apo-HPPK(W89A) at 1.45 Angstrom resolution
Summary
Header TRANSFERASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.45 Å, R-factor: 13.1%, Free R-factor: 17.4%, Spacegroup: P 1 21 1
Released 21/06/2005, deposition: 10/06/2004, last revision: 24/02/2009
Authors Blaszczyk, J.search; Ji, X.search
Primary citation 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.
BIOCHEMISTRYsearch vol:44, pag:8590-8599 (2005) [PubMed ID 15952765 ]search
Keywords PYROPHOSPHOKINASEsearch, PYROPHOSPHORYL TRANSFERsearch, FOLATEsearch, HPPKsearch, 6-HYDROXYMETHYLPTERINsearch, 6-HYDROXYMETHYL-7search, 8-DIHYDROPTERINsearch, ANTIMICROBIAL AGENTsearch, DRUG DESIGNsearch, X-RAY CRYSTALLOGRAPHYsearch, POINT MUTANTsearch, STRUCTURAL MUTAGENESISsearch, TRANSFERASEsearch
EC 2.7.6.3 ExPASy BRENDA search (A)
Organism Escherichia coli 562search(A)
UniProt 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) P26281search (A)
Solvent A
Related entries 1hka, 1eqm, 1eq0, 1q0n, 1ex8, 1cbk, 1dy3, 1f9y, 1f9h, 1g4c, 1hq2, 1im6, 1kbr, 1ru2, 1ru1, 1rtz, 1rb0, 1tmm
Polymers
Id Name Type UniProt Residues Observed
A 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase Protein P26281 (HPPK_ECOLI)search
158 100%
Heterogens
Id Name Ligands
A MAGNESIUM ION MG search
A CHLORIDE ION CL search
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