3mk1

Refinement of placental alkaline phosphatase complexed with nitrophenyl

spinqualitylabelsall models 3mk1, resolution 1.57Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3mk1 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.57Å Ligands: ACT, CA, MG, NA, NAG, NPO, PO4, SEP, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PPB1_HUMAN Publication Abstract from PubMed In order to gain deeper insights into the functional sites of human placental alkaline phosphatase, the structures of the enzyme with the putative regulators L-Phe, pNPP and 5'-AMP [Llinas et al. (2005), J. Mol. Biol. 350, 441-451] were re-refined. Significant variations in ligand positioning and identity were found compared with the previous report. The multiple corrections to the model improved the phases and the electron-density maps, allowing the modeling of omitted side chains and multiple disordered residues. These improvements led to a change in the position of L-Phe at the peripheral binding site, which appeared to be reversed. The structure with pNPP contained only p-nitrophenol in three distinct sites, while the structure with 5'-AMP contained the p-nitrophenyl group in two of the sites instead of 5'-AMP. Comparison of the re-refined models shows a consistent pattern of interactions at the peripheral site. Refined structures of placental alkaline phosphatase show a consistent pattern of interactions at the peripheral site.,Stec B, Cheltsov A, Millan JL Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Aug 1;66(Pt, 8):866-70. Epub 2010 Jul 27. PMID:20693656 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alkaline phosphatase 3D structures

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