2PHA

Crystal structure of native, unliganded human arginase at 1.90 resolution

2PHA の概要

• エントリーDOI: 10.2210/pdb2pha/pdb
• 関連するPDBエントリー: 1WVA 2AEB 2PHO
• 分子名称: Arginase-1, MANGANESE (II) ION (3 entities in total)
• 機能のキーワード: proton wire, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm: P05089
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 69779.51

構造登録者

Di Costanzo, L.,Pique, M.E.,Christianson, D.W. (登録日: 2007-04-10, 公開日: 2007-05-08, 最終更新日: 2023-08-30)

主引用文献

Di Costanzo, L.,Pique, M.E.,Christianson, D.W.
Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster.
J.Am.Chem.Soc., 129:6388-6389, 2007

PubMed Abstract: The crystal structure of the human arginase I-thiosemicarbazide complex reveals an unusual thiocarbonyl μ-sulfide ligand in the binuclear manganese cluster. The C=S moiety of thiosemicarbazide bridges MnA and MnB with coordination distances of 2.6 Å and 2.4 Å, respectively. Otherwise, the binding of thiosemicarbazide to human arginase I does not cause any significant structural changes in the active site. The crystal structure of the unliganded enzyme reveals a hydrogen bonded water molecule that could support proton transfer between a μ-water molecule and H141 to regenerate the nucleophilic μ-hydroxide ion in the final step of catalysis.

PubMed: 17469833
DOI: 10.1021/ja071567j

実験手法

X-RAY DIFFRACTION (1.9 Å)