3F3M
Six Crystal Structures of Two Phosphopantetheine Adenylyltransferases Reveal an Alternative Ligand Binding Mode and an Associated Structural Change
Summary for 3F3M
Entry DOI | 10.2210/pdb3f3m/pdb |
Related | 3F3I 3F3J 3F3L 3F3N 3F3O |
Descriptor | Phosphopantetheine adenylyltransferase, 3'-PHOSPHATE-ADENOSINE-5'-PHOSPHATE SULFATE (3 entities in total) |
Functional Keywords | phosphopantetheine adenylyltransferase, ppat, coenzyme a biosynthetic pathway, coenzyme a biosynthesis, nucleotidyltransferase, transferase |
Biological source | Staphylococcus aureus |
Cellular location | Cytoplasm (By similarity): P63820 |
Total number of polymer chains | 1 |
Total formula weight | 19975.57 |
Authors | Lee, H.H.,Yoon, H.J.,Suh, S.W. (deposition date: 2008-10-31, release date: 2009-10-20, Last modification date: 2023-11-01) |
Primary citation | Lee, H.H.,Yoon, H.J.,Kang, J.Y.,Park, J.H.,Kim, D.J.,Choi, K.H.,Lee, S.K.,Song, J.,Kim, H.J.,Suh, S.W. The structure of Staphylococcus aureus phosphopantetheine adenylyltransferase in complex with 3'-phosphoadenosine 5'-phosphosulfate reveals a new ligand-binding mode Acta Crystallogr.,Sect.F, 65:987-991, 2009 Cited by PubMed: 19851003DOI: 10.1107/S1744309109036616 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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