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 | | Descriptor: | (4R)-2-METHYLPENTANE-2,4-DIOL, (4S)-2-METHYL-2,4-PENTANEDIOL, 2-(4-dodecyl-1H-1,2,3-triazol-1-yl)-5'-O-{[(2-hydroxyphenyl)carbonyl]sulfamoyl}adenosine, ... | | Authors: | Drake, E.J, Duckworth, B.P, Neres, J, Aldrich, C.C, Gulick, A.M. | | Deposit date: | 2010-08-02 | | Release date: | 2010-10-06 | | Last modified: | 2023-09-06 | | Method: | X-RAY DIFFRACTION (1.9 Å) | | Cite: | Biochemical and structural characterization of bisubstrate inhibitors of BasE, the self-standing nonribosomal peptide synthetase adenylate-forming enzyme of acinetobactin synthesis.
Biochemistry, 49, 2010
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3O84
 | | Structure of BasE N-terminal domain from Acinetobacter baumannii bound to 6-phenyl-1-(pyridin-4-ylmethyl)-1H-pyrazolo[3,4-b]pyridine-4-carboxylic acid. | | Descriptor: | (4R)-2-METHYLPENTANE-2,4-DIOL, (4S)-2-METHYL-2,4-PENTANEDIOL, 6-phenyl-1-(pyridin-4-ylmethyl)-1H-pyrazolo[3,4-b]pyridine-4-carboxylic acid, ... | | Authors: | Drake, E.J, Duckworth, B.P, Neres, J, Aldrich, C.C, Gulick, A.M. | | Deposit date: | 2010-08-02 | | Release date: | 2010-10-06 | | Last modified: | 2023-09-06 | | Method: | X-RAY DIFFRACTION (2.1 Å) | | Cite: | Biochemical and structural characterization of bisubstrate inhibitors of BasE, the self-standing nonribosomal peptide synthetase adenylate-forming enzyme of acinetobactin synthesis.
Biochemistry, 49, 2010
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3O82
 | | Structure of BasE N-terminal domain from Acinetobacter baumannii bound to 5'-O-[N-(2,3-dihydroxybenzoyl)sulfamoyl] adenosine | | Descriptor: | 5'-O-{[(2,3-dihydroxyphenyl)carbonyl]sulfamoyl}adenosine, CALCIUM ION, Peptide arylation enzyme | | Authors: | Drake, E.J, Duckworth, B.P, Neres, J, Aldrich, C.C, Gulick, A.M. | | Deposit date: | 2010-08-02 | | Release date: | 2010-10-06 | | Last modified: | 2023-09-06 | | Method: | X-RAY DIFFRACTION (2.7 Å) | | Cite: | Biochemical and structural characterization of bisubstrate inhibitors of BasE, the self-standing nonribosomal peptide synthetase adenylate-forming enzyme of acinetobactin synthesis.
Biochemistry, 49, 2010
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