6ENP

Atomic resolution structure of human RNase 6 in the presence of phosphate anions in P21 space group.

6ENP の概要

• エントリーDOI: 10.2210/pdb6enp/pdb
• 分子名称: Ribonuclease K6, PHOSPHATE ION, ZINC ION, ... (6 entities in total)
• 機能のキーワード: rnase k6, hydrolase, pancreatic ribonuclease
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15261.81

構造登録者

Prats-Ejarque, G.,Moussaoui, M.,Boix, E. (登録日: 2017-10-05, 公開日: 2018-10-24, 最終更新日: 2024-11-13)

主引用文献

Prats-Ejarque, G.,Blanco, J.A.,Salazar, V.A.,Nogues, V.M.,Moussaoui, M.,Boix, E.
Characterization of an RNase with two catalytic centers. Human RNase6 catalytic and phosphate-binding site arrangement favors the endonuclease cleavage of polymeric substrates.
Biochim Biophys Acta Gen Subj, 1863:105-117, 2019

PubMed Abstract: Human RNase6 is a small cationic antimicrobial protein that belongs to the vertebrate RNaseA superfamily. All members share a common catalytic mechanism, which involves a conserved catalytic triad, constituted by two histidines and a lysine (His15/His122/Lys38 in RNase6 corresponding to His12/His119/Lys41 in RNaseA). Recently, our first crystal structure of human RNase6 identified an additional His pair (His36/His39) and suggested the presence of a secondary active site.

PubMed: 30287244
DOI: 10.1016/j.bbagen.2018.09.021

実験手法

X-RAY DIFFRACTION (1.042 Å)