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; PubMed: 20853905; DOI: 10.1021/bi101226n

Experimental method

X-RAY DIFFRACTION (1.9 Å)