3TW2

High resolution structure of human histidine triad nucleotide-binding protein 1 (hHINT1)/AMP complex in a monoclinic space group

3TW2 の概要

• エントリーDOI: 10.2210/pdb3tw2/pdb
• 関連するPDBエントリー: 1AV5 1KPA 1KPB 1KPC 1KPE 1KPF
• 分子名称: Histidine triad nucleotide-binding protein 1, ADENOSINE MONOPHOSPHATE (3 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: Cytoplasm: P49773
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27995.08

構造登録者

Dolot, R.M.,Wlodarczyk, A.,Ozga, M.,Krakowiak, A.,Nawrot, B. (登録日: 2011-09-21, 公開日: 2011-11-02, 最終更新日: 2023-09-13)

主引用文献

Dolot, R.,Ozga, M.,Wlodarczyk, A.,Krakowiak, A.,Nawrot, B.
A new crystal form of human histidine triad nucleotide-binding protein 1 (hHINT1) in complex with adenosine 5'-monophosphate at 1.38 A resolution.
Acta Crystallogr.,Sect.F, 68:883-888, 2012

PubMed Abstract: Histidine triad nucleotide-binding protein 1 (HINT1) represents the most ancient and widespread branch of the histidine triad protein superfamily. HINT1 plays an important role in various biological processes and has been found in many species. Here, the structure of the human HINT1-adenosine 5'-monophosphate (AMP) complex at 1.38 Å resolution obtained from a new monoclinic crystal form is reported. The final structure has R(cryst) = 0.1207 (R(free) = 0.1615) and the model exhibits good stereochemical quality. Detailed analysis of the high-resolution data allowed the details of the protein structure to be updated in comparison to the previously published data.

PubMed: 22869114
DOI: 10.1107/S1744309112029491

実験手法

X-RAY DIFFRACTION (1.38 Å)