1ERQ
X-RAY CRYSTAL STRUCTURE OF TEM-1 BETA LACTAMASE IN COMPLEX WITH A DESIGNED BORONIC ACID INHIBITOR (1R)-1-ACETAMIDO-2-(3-CARBOXY-2-HYDROXYPHENYL)ETHYL BORONIC ACID
Summary for 1ERQ
Entry DOI | 10.2210/pdb1erq/pdb |
Related | 1ERM 1ERO |
Descriptor | TEM-1 BETA-LACTAMASE, 1(R)-1-ACETAMIDO-2-(3-CARBOXY-2-HYDROXYPHENYL)ETHYL BORONIC ACID (3 entities in total) |
Functional Keywords | beta-lactamase, structure-based design, boronate inhibitor, hydrolase |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 29209.04 |
Authors | Ness, S.,Martin, R.,Kindler, A.M.,Paetzel, M.,Gold, M.,Jones, J.B.,Strynadka, N.C.J. (deposition date: 2000-04-06, release date: 2000-05-10, Last modification date: 2011-07-13) |
Primary citation | Ness, S.,Martin, R.,Kindler, A.M.,Paetzel, M.,Gold, M.,Jensen, S.E.,Jones, J.B.,Strynadka, N.C. Structure-based design guides the improved efficacy of deacylation transition state analogue inhibitors of TEM-1 beta-Lactamase(,). Biochemistry, 39:5312-5321, 2000 Cited by PubMed: 10820001DOI: 10.1021/bi992505b PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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