3cz4 | pdb_00003cz4

Native AphA class B acid phosphatase/phosphotransferase from E. coli

spinqualitylabelsall models 3cz4, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3cz4 is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, CL, EDO, MG Related: 1rmq, 1rmy, 1n8n, 1n9k, 2g1a, 2hf7 Gene: aphA, napA, yjbP, b4055, JW4015 (Escherichia coli) Activity: Acid phosphatase, with EC number 3.1.3.2 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 AphA is a magnesium-dependent, bacterial class B acid phosphatase that catalyzes the hydrolysis of a variety of phosphoester substrates and belongs to the DDDD superfamily of phosphohydrolases. The recently reported crystal structure of AphA from Escherichia coli has revealed the quaternary structure of the enzyme together with hints about its catalytic mechanism. The present work reports the crystal structures of AphA from E. coli in complex with substrate, transition-state, and intermediate analogues. The structures provide new insights into the mechanism of the enzyme and allow a revision of some aspects of the previously proposed mechanism that have broader implications for all the phosphatases of the DDDD superfamily. Structural insights into the catalytic mechanism of the bacterial class B phosphatase AphA belonging to the DDDD superfamily of phosphohydrolases.,Leone R, Cappelletti E, Benvenuti M, Lentini G, Thaller MC, Mangani S J Mol Biol. 2008 Dec 12;384(2):478-88. Epub 2008 Sep 27. PMID:18845157 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acid phosphatase

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