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: 29070681 DOI: 10.1074/jbc.M117.788240 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.45 Å)

Structure validation