1AUR

PMSF-INHIBITED CARBOXYLESTERASE FROM PSEUDOMONAS FLUORESCENS

Summary for 1AUR

• Entry DOI: 10.2210/pdb1aur/pdb
• Descriptor: CARBOXYLESTERASE, phenylmethanesulfonic acid (3 entities in total)
• Functional Keywords: hydrolase
• Biological source: Pseudomonas fluorescens
• Total number of polymer chains: 2
• Total formula weight: 48146.89

Authors

Kim, K.K.,Song, H.K.,Suh, S.W. (deposition date: 1997-09-01, release date: 1998-03-04, Last modification date: 2024-11-20)

Primary citation

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

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: 9438866
DOI: 10.1016/S0969-2126(97)00306-7

Experimental method

X-RAY DIFFRACTION (2.5 Å)