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PDBe Entry: 1ecg 
DON INACTIVATED ESCHERICHIA COLI GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE (PRPP) AMIDOTRANSFERASE
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TRANSFERASE (GLUTAMINE AMIDOTRANSFERASE)
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X-RAY DIFFRACTION
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Resolution: 2.3 Å, R-factor: 14.7%, Free R-factor: 22.9%, Spacegroup: C 2 2 21
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08/11/1996, deposition: 23/04/1996, last revision: 24/02/2009
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Krahn, J.M.
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Structure and function of the glutamine phosphoribosylpyrophosphate amidotransferase glutamine site and communication with the phosphoribosylpyrophosphate site. J.BIOL.CHEM. vol:271, pag:15549-15557 (1996) [PubMed ID 8663035 ]
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PURINE BIOSYNTHESIS , TRANSFERASE , GLYCOSYLTRANSFERASE , GLUTAMINE AMIDOTRANSFERASE , TRANSFERASE (GLUTAMINE AMIDOTRANSFERASE)
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2.4.2.14 ExPASy BRENDA (A B)
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Escherichia coli 562 (A B)
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Amidophosphoribosyltransferase (EC 2.4.2.14) (ATase) (Glutamine phosphoribosylpyrophosphate amidotransferase) (GPATase) P0AG16 (A B)
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A, B
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| A, B |
GLUTAMINE PHOSPHORIBOSYLPYROPHOSPHATE AMIDOTRANSFERASE |
Protein |
P0AG16 (PUR1_ECOLI)
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504 |
99% |
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| A, B |
5-OXO-L-NORLEUCINE |
ONL
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| A, B |
PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID) |
PIN
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