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1E21

Ribonuclease 1 des1-7 Crystal Structure at 1.9A

1E21 の概要
エントリーDOI10.2210/pdb1e21/pdb
関連するPDBエントリー1H8X
分子名称RIBONUCLEASE 1 (2 entities in total)
機能のキーワードhuman pancreatic ribonuclease, hydrolase
由来する生物種HOMO SAPIENS (HUMAN)
細胞内の位置Secreted: P07998
タンパク質・核酸の鎖数1
化学式量合計14539.30
構造登録者
主引用文献Pous, J.,Mallorqui-Fernandez, G.,Peracaula, R.,Terzyan, S.S.,Futami, J.,Tada, H.,Yamada, H.,Seno, M.,De Llorens, R.,Gomis-Ruth, F.X.,Coll, M.
Three-Dimensional Crystal Structure of Human Rnase 1Dn7 at 1.9A Resolution
Acta Crystallogr.,Sect.D, 57:498-, 2001
Cited by
PubMed Abstract: Human pancreatic ribonuclease 1 (RNase 1) is considered to be the human counterpart of bovine pancreatic RNase A. Truncation of seven amino-acid residues from the amino-terminal sequence resulted in RNase 1 Delta N7, which has a reduced ribonucleolytic activity and a lower affinity for the human placental RNase inhibitor (PRI). This RNase 1 variant has been cloned, heterologously overexpressed, purified and crystallized. Its crystal structure has been determined and refined using data to 1.9 A resolution. The molecule displays the alpha + beta folding topology typical of members of the RNase A superfamily. The main distinct features found in RNase 1 Delta N7 are basically located in three loops affecting the fitting of the enzyme to the active site of subtilisin and the shape of the B2 subsite. These changes, taken with the lack of the catalytically active residue Lys7, may explain the reduced affinity of RNase 1 Delta N7 for PRI and the low ribonucleolytic activity of the protein when compared with the native enzyme.
PubMed: 11264578
DOI: 10.1107/S0907444901001147
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.9 Å)
構造検証レポート
Validation report summary of 1e21
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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