2vi7 | pdb_00002vi7

Structure of a Putative Acetyltransferase (PA1377)from Pseudomonas aeruginosa

spinqualitylabelsall models 2vi7, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vi7 is a 3 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. Ligands: AZI, GOL, SO4 Activity: Glucokinase, with EC number 2.7.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum 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 PA1377 from Pseudomonas aeruginosa encodes a 177-amino-acid conserved hypothetical protein of unknown function. The structure of this protein (termed pitax) has been solved in space group I222 to 2.25 A resolution. Pitax belongs to the GCN5-related N-acetyltransferase family and contains all four sequence motifs conserved among family members. The beta-strand structure in one of these motifs (motif A) is disrupted, which is believed to affect binding of the substrate that accepts the acetyl group from acetyl-CoA. Structure of a putative acetyltransferase (PA1377) from Pseudomonas aeruginosa.,Davies AM, Tata R, Chauviac FX, Sutton BJ, Brown PR Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 May 1;64(Pt 5):338-42., Epub 2008 Apr 24. PMID:18453699 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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