Summary for 1VM1
| Entry DOI | 10.2210/pdb1vm1/pdb |
| Related | 1SHV |
| Descriptor | BETA-LACTAMASE SHV-1, CYCLOHEXYL-HEXYL-BETA-D-MALTOSIDE, TAZOBACTAM INTERMEDIATE, ... (6 entities in total) |
| Functional Keywords | beta-lactamase, beta-lactam hydrolase, penicillinase, detergent binding, inhibitor design, hydrolase |
| Biological source | Klebsiella pneumoniae |
| Total number of polymer chains | 1 |
| Total formula weight | 30598.88 |
| Authors | Kuzin, A.P.,Nukaga, M.,Nukaga, Y.,Hujer, A.,Bonomo, R.A.,Knox, J.R. (deposition date: 2004-08-27, release date: 2004-09-07, Last modification date: 2025-05-07) |
| Primary citation | Kuzin, A.P.,Nukaga, M.,Nukaga, Y.,Hujer, A.,Bonomo, R.A.,Knox, J.R. Inhibition of the SHV-1 beta-lactamase by sulfones: crystallographic observation of two reaction intermediates with tazobactam. Biochemistry, 40:1861-1866, 2001 Cited by PubMed Abstract: Two species resulting from the reaction of the SHV-1 class A beta-lactamase with the sulfone inhibitor tazobactam have been trapped at 100 K and mapped by X-ray crystallography at 2.0 A resolution. An acyclic form of tazobactam is covalently bonded to the catalytic Ser70 side chain, and a second species, a five-atom vinyl carboxylic acid fragment of tazobactam, is bonded to Ser130. It is proposed that the electron density map of the crystal is a composite picture of two complexes, each with only a single bound species. It is estimated that the two complexes exist in the crystal in approximately equal populations. Results are discussed in relation to the mechanism-based inhibition of class A beta-lactamases by the similar inhibitors sulbactam and clavulanic acid. PubMed: 11327849DOI: 10.1021/bi0022745 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.02 Å) |
Structure validation
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