3O83
Structure of BasE N-terminal domain from Acinetobacter baumannii bound to 2-(4-n-dodecyl-1,2,3-triazol-1-yl)-5'-O-[N-(2-hydroxybenzoyl)sulfamoyl]adenosine
Summary for 3O83
Entry DOI | 10.2210/pdb3o83/pdb |
Related | 3O82 3O84 |
Descriptor | Peptide arylation enzyme, 2-(4-dodecyl-1H-1,2,3-triazol-1-yl)-5'-O-{[(2-hydroxyphenyl)carbonyl]sulfamoyl}adenosine, CALCIUM ION, ... (6 entities in total) |
Functional Keywords | ligase, adenylation of 2, 3-dihydroxybenzoate and transfer to pantetheine cofactor of basf, non-ribosomal peptide synthetase (nrps) |
Biological source | Acinetobacter baumannii |
Total number of polymer chains | 2 |
Total formula weight | 123616.94 |
Authors | Drake, E.J.,Duckworth, B.P.,Neres, J.,Aldrich, C.C.,Gulick, A.M. (deposition date: 2010-08-02, release date: 2010-10-06, Last modification date: 2023-09-06) |
Primary citation | Drake, E.J.,Duckworth, B.P.,Neres, J.,Aldrich, C.C.,Gulick, A.M. Biochemical and structural characterization of bisubstrate inhibitors of BasE, the self-standing nonribosomal peptide synthetase adenylate-forming enzyme of acinetobactin synthesis. Biochemistry, 49:9292-9305, 2010 Cited by PubMed: 20853905DOI: 10.1021/bi101226n PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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