Structural highlights 
| 4bd1 is a 1 chain structure with sequence from Ecobb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. 
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| Ligands: | , | 
| Related: | 1bza, 1iyo, 1iyp, 1iyq, 1iys, 1we4, 2wyx, 2xqz, 2xr0, 4bd0 | 
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | 
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT | 
  Function 
[BLT1_ECOLX] Has strong cefotaxime-hydrolyzing activity. 
  Publication Abstract from PubMed 
The mechanism by which class A beta-lactamase enzymes form an acyl-enzyme intermediate has been the emphasis of several studies. Here, we report on the use of neutron and high resolution X-ray diffraction to help elucidate the identity of the catalytic base in the acylation part of the mechanism.
Neutron and X-ray crystal structures of a perdeuterated enzyme inhibitor complex reveal the catalytic proton network of the Toho-1 beta-lactamase for the acylation reaction.,Tomanicek SJ, Standaert RF, Weiss KL, Ostermann A, Schrader TE, Ng JD, Coates L J Biol Chem. 2012 Dec 18. PMID:23255594[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
 
 See Also
  References 
- ↑ Tomanicek SJ, Standaert RF, Weiss KL, Ostermann A, Schrader TE, Ng JD, Coates L. Neutron and X-ray crystal structures of a perdeuterated enzyme inhibitor complex  reveal the catalytic proton network of the Toho-1 beta-lactamase for the acylation reaction. J Biol Chem. 2012 Dec 18. PMID:23255594 doi:http://dx.doi.org/10.1074/jbc.M112.436238