5TPQ
E. coli alkaline phosphatase D101A, D153A, R166S, E322A, K328A mutant
Summary for 5TPQ
Entry DOI | 10.2210/pdb5tpq/pdb |
Related | 3TG0 |
Descriptor | Alkaline phosphatase, ZINC ION, PHOSPHATE ION, ... (4 entities in total) |
Functional Keywords | alkaline phosphatase, generalist enzyme, bimetallo motif, catalytic promiscuity, evolution, d101a/d153a/r166s/e322a/k328a, hydrolase |
Biological source | Escherichia coli (strain K12) |
Total number of polymer chains | 2 |
Total formula weight | 93769.29 |
Authors | Sunden, F.,AlSadhan, I.,Lyubimov, A.Y.,Doukov, T.,Swan, J.,Herschlag, D. (deposition date: 2016-10-20, release date: 2017-11-01, Last modification date: 2023-10-04) |
Primary citation | Sunden, F.,AlSadhan, I.,Lyubimov, A.,Doukov, T.,Swan, J.,Herschlag, D. Differential catalytic promiscuity of the alkaline phosphatase superfamily bimetallo core reveals mechanistic features underlying enzyme evolution. J. Biol. Chem., 292:20960-20974, 2017 Cited by PubMed: 29070681DOI: 10.1074/jbc.M117.788240 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
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