6JZL

S-formylglutathione hydrolase homolog from a psychrophilic bacterium of Shewanella frigidimarina

Summary for 6JZL

• Entry DOI: 10.2210/pdb6jzl/pdb
• Descriptor: S-formylglutathione hydrolase (2 entities in total)
• Functional Keywords: s-formylglutathione hydrolase, shewanella frigidimarina, hydrolase
• Biological source: Shewanella frigidimarina
• Total number of polymer chains: 2
• Total formula weight: 62133.93

Authors

Lee, C.W.,Lee, J.H. (deposition date: 2019-05-02, release date: 2019-09-04, Last modification date: 2024-03-27)

Primary citation

Lee, C.W.,Yoo, W.,Park, S.H.,Le, L.T.H.L.,Jeong, C.S.,Ryu, B.H.,Shin, S.C.,Kim, H.W.,Park, H.,Kim, K.K.,Kim, T.D.,Lee, J.H.
Structural and functional characterization of a novel cold-active S-formylglutathione hydrolase (SfSFGH) homolog from Shewanella frigidimarina, a psychrophilic bacterium.
Microb. Cell Fact., 18:140-140, 2019

PubMed Abstract: S-Formylglutathione is hydrolyzed to glutathione and formate by an S-formylglutathione hydrolase (SFGH) (3.1.2.12). This thiol esterase belongs to the esterase family and is also known as esterase D. SFGHs contain highly conserved active residues of Ser-Asp-His as a catalytic triad at the active site. Characterization and investigation of SFGH from Antarctic organisms at the molecular level is needed for industrial use through protein engineering.

PubMed: 31426813
DOI: 10.1186/s12934-019-1190-1

Experimental method

X-RAY DIFFRACTION (2.32 Å)