7C9M
The structure of product-bound CntL, an aminobutyrate transferase in staphylopine biosynthesis
Summary for 7C9M
Entry DOI | 10.2210/pdb7c9m/pdb |
Descriptor | D-histidine 2-aminobutanoyltransferase, (2S)-2-azanyl-4-[[(2R)-3-(1H-imidazol-4-yl)-1-oxidanyl-1-oxidanylidene-propan-2-yl]amino]butanoic acid, 5'-DEOXY-5'-METHYLTHIOADENOSINE, ... (4 entities in total) |
Functional Keywords | metallophore, biosynthesis, product, aminobutyrate, transferase |
Biological source | Staphylococcus aureus subsp. aureus Mu50 |
Total number of polymer chains | 4 |
Total formula weight | 129650.36 |
Authors | |
Primary citation | Luo, Z.,Luo, S.,Ju, Y.,Ding, P.,Xu, J.,Gu, Q.,Zhou, H. Structural insights into the ligand recognition and catalysis of the key aminobutanoyltransferase CntL in staphylopine biosynthesis. Faseb J., 35:e21575-e21575, 2021 Cited by PubMed: 33826776DOI: 10.1096/fj.202002287RR PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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