7C29

Esterase CrmE10 mutant-D178A

Replaces:  6M42Replaces:  6IQ8

Summary for 7C29

• Entry DOI: 10.2210/pdb7c29/pdb
• Descriptor: Carboxylesterase, 1,2-ETHANEDIOL, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: esterase crme10 mutant-d178a, hydrolase
• Biological source: Croceicoccus marinus
• Total number of polymer chains: 2
• Total formula weight: 45060.36

Authors

Li, Z.,Li, J. (deposition date: 2020-05-07, release date: 2020-05-20, Last modification date: 2023-11-29)

Primary citation

Li, Z.,Li, L.,Huo, Y.,Chen, Z.,Zhao, Y.,Huang, J.,Jian, S.,Rong, Z.,Wu, D.,Gan, J.,Hu, X.,Li, J.,Xu, X.W.
Structure-guided protein engineering increases enzymatic activities of the SGNH family esterases.
Biotechnol Biofuels, 13:107-107, 2020

PubMed Abstract: Esterases and lipases hydrolyze short-chain esters and long-chain triglycerides, respectively, and therefore play essential roles in the synthesis and decomposition of ester bonds in the pharmaceutical and food industries. Many SGNH family esterases share high similarity in sequences. However, they have distinct enzymatic activities toward the same substrates. Due to a lack of structural information, the detailed catalytic mechanisms of these esterases remain barely investigated.

PubMed: 32549911
DOI: 10.1186/s13068-020-01742-8

Experimental method

X-RAY DIFFRACTION (2.18 Å)