1HJK
ALKALINE PHOSPHATASE MUTANT H331Q
Summary for 1HJK
Entry DOI | 10.2210/pdb1hjk/pdb |
Descriptor | ALKALINE PHOSPHATASE, ZINC ION, MAGNESIUM ION, ... (5 entities in total) |
Functional Keywords | alkaline phosphatase, hydrolase, phosphoric monoester, transferase(phospho, alcohol acceptor) |
Biological source | Escherichia coli |
Cellular location | Periplasm: P00634 |
Total number of polymer chains | 2 |
Total formula weight | 94831.09 |
Authors | Murphy, J.E.,Stec, B.,Ma, L.,Kantrowitz, E.R. (deposition date: 1997-05-30, release date: 1997-10-15, Last modification date: 2024-11-13) |
Primary citation | Murphy, J.E.,Stec, B.,Ma, L.,Kantrowitz, E.R. Trapping and visualization of a covalent enzyme-phosphate intermediate. Nat.Struct.Biol., 4:618-622, 1997 Cited by PubMed Abstract: Using a mutant version of E. coli alkaline phosphatase, we succeeded in trapping and determining the structure of the phospho-enzyme intermediate. The X-ray structure also revealed the catalytic water molecule, bound to one of the active site zinc ions, positioned ideally for the apical attack necessary for the hydrolysis of the intermediate. PubMed: 9253408DOI: 10.1038/nsb0897-618 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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