3MK1

Refinement of placental alkaline phosphatase complexed with nitrophenyl

3MK1 の概要

• エントリーDOI: 10.2210/pdb3mk1/pdb
• 関連するPDBエントリー: 3MK0 3MK2
• 分子名称: 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)
• 機能のキーワード: hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cell membrane; Lipid-anchor, GPI-anchor: P05187
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 54709.94

構造登録者

Stec, B.,Cheltsov, A.,Millan, J.L. (登録日: 2010-04-13, 公開日: 2011-01-19, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.57 Å)