3IAQ
E. coli (lacz) beta-galactosidase (E416V)
Summary for 3IAQ
| Entry DOI | 10.2210/pdb3iaq/pdb |
| Related | 1DP0 3DYM 3DYP 3IAP |
| Descriptor | Beta-galactosidase, MAGNESIUM ION, SODIUM ION, ... (6 entities in total) |
| Functional Keywords | glu-416-val beta-galactosidase hydrolase tim barrel(alpha/beta barrel) jelly-roll barrel immunoglobulin beta supersandwhich, glycosidase, hydrolase |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 4 |
| Total formula weight | 474490.01 |
| Authors | Lo, S.,Dugdale, M.L.,Jeerh, N.,Ku, T.,Roth, N.J.,Huber, R.E. (deposition date: 2009-07-14, release date: 2009-12-29, Last modification date: 2023-09-06) |
| Primary citation | Lo, S.,Dugdale, M.L.,Jeerh, N.,Ku, T.,Roth, N.J.,Huber, R.E. 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., 29:26-31, 2010 Cited by PubMed: 19936901DOI: 10.1007/s10930-009-9216-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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