Brand  (β version)

PDB ID: 3O83

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Ligands
Code Name Style Show Link
IXN 2-(4-dodecyl-1h-1,2,3-triazol-1-yl)-5'-O-{[(2-hydroxyphenyl)carbonyl]sulfamoyl}adenosine PoSSuM
CA Calcium ion PoSSuM
MPD (4s)-2-methyl-2,4-pentanediol PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 3O83   PDBj   RCSB PDB   PDBe
Header : LIGASE
Title : 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
Release Data : 2010-10-06
Compound :
mol_id molecule chains
1 Peptide arylation enzyme A,B
ec: 6.2.1.-
fragment: BasE
mutation: P45L
Source :
mol_id organism_scientific expression_system
1 Acinetobacter baumannii  (taxid:557601) Escherichia coli  (taxid:469008)
strain: AB900
gene: ACICU_02578, basE
expression_system_strain: BL21(DE3)
expression_system_vector_type: plasmid
expression_system_plasmid: pED453
Authors : Drake, E.J., Duckworth, B.P., Neres, J., Aldrich, C.C., Gulick, A.M.
Keywords : Ligase, Adenylation of 2, 3-dihydroxybenzoate and transfer to pantetheine cofactor of BasF, Non-Ribosomal Peptide Synthetase (NRPS)
Exp. method : X-RAY DIFFRACTION ( 1.90 Å )
Citation :

Biochemical and structural characterization of bisubstrate inhibitors of BasE, the self-standing nonribosomal peptide synthetase adenylate-forming enzyme of acinetobactin synthesis.

Drake, E.J.,Duckworth, B.P.,Neres, J.  et al.
(2010)  Biochemistry  49 : 9292 - 9305

PubMed: 20853905
DOI: 10.1021/bi101226n

Reaction

Chain : A, B
UniProt : B2HVG8
Reaction : -