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: 2024-05-29) |
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 Cited by PubMed: 20059543DOI: 10.1111/j.1742-4658.2009.07515.x PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
Download full validation report