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.

Summary for 3O84

• Entry DOI: 10.2210/pdb3o84/pdb
• Related: 3O82 3O83
• Descriptor: Peptide arylation enzyme, 6-phenyl-1-(pyridin-4-ylmethyl)-1H-pyrazolo[3,4-b]pyridine-4-carboxylic acid, CALCIUM ION, ... (7 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: 122944.05

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 (2.1 Å)