6ASV
E. coli PRPP Synthetase
Summary for 6ASV
Entry DOI | 10.2210/pdb6asv/pdb |
Descriptor | Ribose-phosphate pyrophosphokinase, PHOSPHATE ION, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | nucleotide biosynthesis phosphoribosyl pyrophosphate kprs, transferase |
Biological source | Escherichia coli O157:H7 |
Total number of polymer chains | 3 |
Total formula weight | 109920.45 |
Authors | French, J.B.,Zhou, W. (deposition date: 2017-08-25, release date: 2019-01-23, Last modification date: 2023-10-04) |
Primary citation | Zhou, W.,Tsai, A.,Dattmore, D.A.,Stives, D.P.,Chitrakar, I.,D'alessandro, A.M.,Patil, S.,Hicks, K.A.,French, J.B. Crystal structure of E. coli PRPP synthetase. BMC Struct. Biol., 19:1-1, 2019 Cited by PubMed Abstract: Ribose-phosphate pyrophosphokinase (EC 2.7.6.1) is an enzyme that catalyzes the ATP-dependent conversion of ribose-5-phosphate to phosphoribosyl pyrophosphate. The reaction product is a key precursor for the biosynthesis of purine and pyrimidine nucleotides. PubMed: 30646888DOI: 10.1186/s12900-019-0100-4 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.21 Å) |
Structure validation
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