3IAP
 
 | | E. coli (lacZ) beta-galactosidase (E416Q) | | Descriptor: | 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, Beta-galactosidase, DIMETHYL SULFOXIDE, ... | | Authors: | Lo, S, Dugdale, M.L, Jeerh, N, Ku, T, Roth, N.J, Huber, R.E. | | Deposit date: | 2009-07-14 | | Release date: | 2009-12-29 | | Last modified: | 2023-09-06 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | Studies of Glu-416 variants of beta-galactosidase (E. coli) show that the active site Mg(2+) is not important for structure and indicate that the main role of Mg (2+) is to mediate optimization of active site chemistry
Protein J., 29, 2010
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3IAQ
 | | E. coli (lacz) beta-galactosidase (E416V) | | Descriptor: | 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, Beta-galactosidase, DIMETHYL SULFOXIDE, ... | | Authors: | Lo, S, Dugdale, M.L, Jeerh, N, Ku, T, Roth, N.J, Huber, R.E. | | Deposit date: | 2009-07-14 | | Release date: | 2009-12-29 | | Last modified: | 2023-09-06 | | Method: | X-RAY DIFFRACTION (2.7 Å) | | Cite: | Studies of Glu-416 variants of beta-galactosidase (E. coli) show that the active site Mg(2+) is not important for structure and indicate that the main role of Mg (2+) is to mediate optimization of active site chemistry
Protein J., 29, 2010
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