5K9N

Structural and Mechanistic Analysis of Drosophila melanogaster Polyamine N acetyltransferase, an enzyme that Catalyzes the Formation of N acetylagmatine

Summary for 5K9N

• Entry DOI: 10.2210/pdb5k9n/pdb
• Descriptor: Polyamine N acetyltransferase (2 entities in total)
• Functional Keywords: polyamine n acetyltransferase, agmatine, n acetylagmatine, drosophila melanogaster, enzyme mechanism, acetyl-coa, and protein crystallography, transferase
• Biological source: Drosophila melanogaster (Fruit fly)
• Total number of polymer chains: 2
• Total formula weight: 47598.22

Authors

Dempsey, D.R.,Nichols, D.A.,Battistini, M.R.,Pemberton, O.,Ospina, S.R.,Zhang, X.,Carpenter, A.-M.,Chen, Y.,Merkler, D.J. (deposition date: 2016-06-01, release date: 2017-06-07, Last modification date: 2024-02-28)

• Primary citation: Dempsey, D.R.,Nichols, D.A.,Battistini, M.R.,Pemberton, O.,Ospina, S.R.,Zhang, X.,Carpenter, A.M.,O'Flynn, B.G.,Leahy, J.W.,Kanwar, A.,Lewandowski, E.M.,Chen, Y.,Merkler, D.J.; Structural and Mechanistic Analysis of Drosophila melanogaster Agmatine N-Acetyltransferase, an Enzyme that Catalyzes the Formation of N-Acetylagmatine.; Sci Rep, 7:13432-13432, 2017; PubMed: 29044148; DOI: 10.1038/s41598-017-13669-6

Experimental method

X-RAY DIFFRACTION (2.3 Å)