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DOI | 10.2210/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: 8087555DOI: 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) |
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