3ZYT
Structure Determination of EstA from Arthrobacter nitroguajacolicus Rue61a
Summary for 3ZYT
| Entry DOI | 10.2210/pdb3zyt/pdb |
| Descriptor | ESTERASE A, ETHYL MERCURY ION (3 entities in total) |
| Functional Keywords | hydrolase, enzymatic promiscuity, beta-lactamase |
| Biological source | ARTHROBACTER NITROGUAJACOLICUS |
| Total number of polymer chains | 1 |
| Total formula weight | 40312.69 |
| Authors | Wagner, U.G.,Fetzner, S. (deposition date: 2011-08-25, release date: 2012-09-19, Last modification date: 2024-05-08) |
| Primary citation | Wagner, U.G.,Dimaio, F.,Kolkenbrock, S.,Fetzner, S. Crystal Structure Analysis of Esta from Arthrobacter Sp. Rue61A--an Insight Into Catalytic Promiscuity. FEBS Lett., 588:1154-, 2014 Cited by PubMed Abstract: In this article we analyze the reasons for catalytic promiscuity of a type VIII esterase with β-lactamase fold and the ability to cleave β-lactams. We compared the structure of this enzyme to those of an esterase of the same type without any lactamase ability, an esterase with moderate lactamase ability, and a class C β-lactamase with similar fold. Our results show that for these enzymes, the difference in the substrate specificity is sterically driven. PubMed: 24613918DOI: 10.1016/J.FEBSLET.2014.02.045 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.45 Å) |
Structure validation
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