2PVQ

Crystal structure of Ochrobactrum anthropi glutathione transferase Cys10Ala mutant with glutathione bound at the H-site

Summary for 2PVQ

• Entry DOI: 10.2210/pdb2pvq/pdb
• Related: 2NTO
• Descriptor: glutathione S-transferase, SULFATE ION, GLUTATHIONE, ... (4 entities in total)
• Functional Keywords: xenobiotics detoxification, glutathione, h-site, transferase
• Biological source: Ochrobactrum anthropi
• Cellular location: Cytoplasm (By similarity): P81065
• Total number of polymer chains: 1
• Total formula weight: 22231.21

Authors

Allocati, N.,Federici, L.,Masulli, M.,Favaloro, B.,Di Ilio, C. (deposition date: 2007-05-10, release date: 2008-01-15, Last modification date: 2023-08-30)

• Primary citation: Allocati, N.,Federici, L.,Masulli, M.,Favaloro, B.,Di Ilio, C.; Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site.; Proteins, 71:16-23, 2008; PubMed: 18076047; DOI: 10.1002/prot.21835

Experimental method

X-RAY DIFFRACTION (1.803 Å)