7C85

Esterase AlinE4 mutant-S13A

Summary for 7C85

Entry DOI	10.2210/pdb7c85/pdb
Descriptor	SGNH-hydrolase family esterase, CADMIUM ION, ACETATE ION, ... (4 entities in total)
Functional Keywords	esterase, sgnh-hydrolase family, marine, hydrolase
Biological source	Altererythrobacter indicus
Total number of polymer chains	1
Total formula weight	21425.23
Authors	Li, Z.,Li, J. (deposition date: 2020-05-28, release date: 2020-07-08, 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 Cited by 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 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.75 Å)

Structure validation