2jlm

Structure of a Putative Acetyltransferase (ACIAD1637) from Acinetobacter baylyi ADP1

spinqualitylabelsall models 2jlm, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2jlm is a 6 chain structure with sequence from Acinetobacter baylyi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.35Å Ligands: ACT, AZI, NA, PEG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6FBS8_ACIAD Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Gene ACIAD1637 from Acinetobacter baylyi ADP1 encodes a 182 amino acid putative antibiotic resistance protein. The structure of this protein (termed acepita) has been solved in space group P(2) to 2.35 A resolution. Acepita belongs to the GCN5-related N-acetyltransferase (GNAT) family, and contains the four sequence motifs conserved among family members. The structure of acepita is compared with that of pita, its homologue from Pseudomonas aeruginosa. Acepita has a similar substrate profile to pita and performs a similar function. Structure and substrate specificity of acetyltransferase ACIAD1637 from Acinetobacter baylyi ADP1.,Davies AM, Tata R, Snape A, Sutton BJ, Brown PR Biochimie. 2009 Apr;91(4):484-9. Epub 2008 Dec 24. PMID:19135125 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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