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1AMP

CRYSTAL STRUCTURE OF AEROMONAS PROTEOLYTICA AMINOPEPTIDASE: A PROTOTYPICAL MEMBER OF THE CO-CATALYTIC ZINC ENZYME FAMILY

1AMP の概要
エントリーDOI10.2210/pdb1amp/pdb
分子名称AMINOPEPTIDASE, ZINC ION (3 entities in total)
機能のキーワードhydrolase(aminopeptidase)
由来する生物種Vibrio proteolyticus
細胞内の位置Secreted: Q01693
タンパク質・核酸の鎖数1
化学式量合計31558.17
構造登録者
Chevrier, B.,Schalk, C.,D'Orchymont, H.,Rondeau, J.M.,Moras, D.,Tarnus, C. (登録日: 1994-04-22, 公開日: 1994-08-31, 最終更新日: 2024-10-30)
主引用文献Chevrier, B.,Schalk, C.,D'Orchymont, H.,Rondeau, J.M.,Moras, D.,Tarnus, C.
Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family.
Structure, 2:283-291, 1994
Cited by
PubMed Abstract: Aminopeptidases specifically cleave the amino-terminal residue from polypeptide chains and are involved in the metabolism of biologically active peptides. The family includes zinc-dependent enzymes possessing either one or two zinc ions per active site. Structural studies providing a detailed view of the metal environment may reveal whether the one-zinc and two-zinc enzymes constitute structurally and mechanistically distinct subclasses, and what role the metal ions play in the catalytic process.
PubMed: 8087555
DOI: 10.1016/S0969-2126(00)00030-7
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.8 Å)
構造検証レポート
Validation report summary of 1amp
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2026-03-04に公開中

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