1AUR
PMSF-INHIBITED CARBOXYLESTERASE FROM PSEUDOMONAS FLUORESCENS
1AUR の概要
| エントリーDOI | 10.2210/pdb1aur/pdb |
| 分子名称 | CARBOXYLESTERASE, phenylmethanesulfonic acid (3 entities in total) |
| 機能のキーワード | hydrolase |
| 由来する生物種 | Pseudomonas fluorescens |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 48146.89 |
| 構造登録者 | |
| 主引用文献 | Kim, K.K.,Song, H.K.,Shin, D.H.,Hwang, K.Y.,Choe, S.,Yoo, O.J.,Suh, S.W. Crystal structure of carboxylesterase from Pseudomonas fluorescens, an alpha/beta hydrolase with broad substrate specificity. Structure, 5:1571-1584, 1997 Cited by PubMed Abstract: A group of esterases, classified as carboxylesterases, hydrolyze carboxylic ester bonds with relatively broad substrate specificity and are useful for stereospecific synthesis and hydrolysis of esters. One such carboxylesterase from Pseudomonas fluorescens is a homodimeric enzyme, consisting of 218-residue subunits. It shows a limited sequence similarity to some members of the alpha/beta hydrolase superfamily. Although crystal structures of a number of serine esterases and lipases have been reported, structural information on carboxylesterases is very limited. This study was undertaken in order to provide such information and to understand a structural basis for the substrate specificity of this carboxylesterase. PubMed: 9438866DOI: 10.1016/S0969-2126(97)00306-7 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.5 Å) |
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