3V16
An intramolecular pi-cation latch in phosphatidylinositol-specific phospholipase C from S.aureus controls substrate access to the active site
Summary for 3V16
Entry DOI | 10.2210/pdb3v16/pdb |
Descriptor | 1-phosphatidylinositol phosphodiesterase, 1,2,3,4,5,6-HEXAHYDROXY-CYCLOHEXANE, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | pi-cation, tim barrel, phospholipase, lyase |
Biological source | Staphylococcus aureus subsp. aureus |
Total number of polymer chains | 1 |
Total formula weight | 34499.77 |
Authors | Goldstein, R.I.,Cheng, J.,Stec, B.,Roberts, M.F. (deposition date: 2011-12-09, release date: 2012-04-04, Last modification date: 2023-09-13) |
Primary citation | Goldstein, R.,Cheng, J.,Stec, B.,Roberts, M.F. Structure of the S. aureus PI-Specific Phospholipase C Reveals Modulation of Active Site Access by a Titratable PI-Cation Latched Loop Biochemistry, 51:2579-2587, 2012 Cited by PubMed: 22390775DOI: 10.1021/bi300057q PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
Download full validation report