3MK1

Refinement of placental alkaline phosphatase complexed with nitrophenyl

Summary for 3MK1

• Entry DOI: 10.2210/pdb3mk1/pdb
• Related: 3MK0 3MK2
• Descriptor: Alkaline phosphatase, placental type, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ZINC ION, ... (10 entities in total)
• Functional Keywords: hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Lipid-anchor, GPI-anchor: P05187
• Total number of polymer chains: 1
• Total formula weight: 54709.94

Authors

Stec, B.,Cheltsov, A.,Millan, J.L. (deposition date: 2010-04-13, release date: 2011-01-19, Last modification date: 2024-11-06)

Primary citation

Stec, B.,Cheltsov, A.,Millan, J.L.
Refined structures of placental alkaline phosphatase show a consistent pattern of interactions at the peripheral site.
Acta Crystallogr.,Sect.F, 66:866-870, 2010

PubMed Abstract: 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.

PubMed: 20693656
DOI: 10.1107/S1744309110019767

Experimental method

X-RAY DIFFRACTION (1.57 Å)