7AAK

Human porphobilinogen deaminase R173W mutant crystallized in the ES2 intermediate state

7AAK の概要

• エントリーDOI: 10.2210/pdb7aak/pdb
• 関連するPDBエントリー: 7AAJ
• 分子名称: Porphobilinogen deaminase, 3-[4-(2-hydroxy-2-oxoethyl)-5-[[4-(2-hydroxy-2-oxoethyl)-5-[[4-(2-hydroxy-2-oxoethyl)-5-[[4-(2-hydroxy-2-oxoethyl)-3-(3-hydroxy-3-oxopropyl)-5-methyl-1~{H}-pyrrol-2-yl]methyl]-3-(3-hydroxy-3-oxopropyl)-1~{H}-pyrrol-2-yl]methyl]-3-(3-hydroxy-3-oxopropyl)-1~{H}-pyrrol-2-yl]methyl]-1~{H}-pyrrol-3-yl]propanoic acid, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: pbg-d, hydroxymethylbilane synthase, hmbs, porphobilinogen deaminase, heme biosynthesis, porphyria, acute intermittent porphyria, es2, reaction intermediate, transferase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 81158.31

構造登録者

Kallio, J.P.,Bustad, H.J.,Martinez, A. (登録日: 2020-09-04, 公開日: 2021-02-17, 最終更新日: 2024-05-01)

• 主引用文献: Bustad, H.J.,Kallio, J.P.,Laitaoja, M.,Toska, K.,Kursula, I.,Martinez, A.,Janis, J.; Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism.; Iscience, 24:102152-102152, 2021; PubMed: 33665570; DOI: 10.1016/j.isci.2021.102152

実験手法

X-RAY DIFFRACTION (1.7 Å)