3GUZ

Structural and substrate-binding studies of pantothenate synthenate (PS)provide insights into homotropic inhibition by pantoate in PS's

Summary for 3GUZ

• Entry DOI: 10.2210/pdb3guz/pdb
• Descriptor: Pantothenate synthetase, PANTOATE (3 entities in total)
• Functional Keywords: pantothenate biosynthesis, substrate binding, competitive inhibition, rossmann fold, non-canonical pantoate binding-site, atp-binding, cytoplasm, ligase, nucleotide-binding
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (Potential): P31663
• Total number of polymer chains: 2
• Total formula weight: 40159.81

Authors

Chakrabarti, K.S.,Thakur, K.G.,Gopal, B.,Sarma, S.P. (deposition date: 2009-03-30, release date: 2010-02-09, Last modification date: 2021-11-10)

• Primary citation: Chakrabarti, K.S.,Thakur, K.G.,Gopal, B.,Sarma, S.P.; X-ray crystallographic and NMR studies of pantothenate synthetase provide insights into the mechanism of homotropic inhibition by pantoate; Febs J., 277:697-712, 2010; PubMed: 20059543; DOI: 10.1111/j.1742-4658.2009.07515.x

Experimental method

X-RAY DIFFRACTION (1.67 Å)