3S22

AMP-C BETA-LACTAMASE (PSEUDOMONAS AERUGINOSA) in complex with an inhibitor

Summary for 3S22

• Entry DOI: 10.2210/pdb3s22/pdb
• Related: 2WZX 2WZZ 3S1Y
• Descriptor: Beta-lactamase, [(2S,3R)-2-formyl-1-{[4-(methylamino)butyl]carbamoyl}pyrrolidin-3-yl]sulfamic acid, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: hydrolase, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• Biological source: Pseudomonas aeruginosa
• Cellular location: Periplasm (By similarity): P24735
• Total number of polymer chains: 1
• Total formula weight: 40995.68

Authors

Scapin, G.,Lu, J.,Fitzgerald, P.M.D.,Sharma, N. (deposition date: 2011-05-16, release date: 2011-06-29, Last modification date: 2024-10-30)

Primary citation

Chen, H.,Blizzard, T.A.,Kim, S.,Wu, J.,Young, K.,Park, Y.W.,Ogawa, A.M.,Raghoobar, S.,Painter, R.E.,Wisniewski, D.,Hairston, N.,Fitzgerald, P.,Sharma, N.,Scapin, G.,Lu, J.,Hermes, J.,Hammond, M.L.
Side chain SAR of bicyclic Beta-lactamase inhibitors (BLIs). 2. N-Alkylated and open chain analogs of MK-8712
Bioorg.Med.Chem.Lett., 21:4267-4270, 2011

PubMed Abstract: The bridged monobactam β-lactamase inhibitor MK-8712 (1) effectively inhibits class C β-lactamases. Side chain N-alkylated and ring-opened analogs of 1 were prepared and evaluated for combination with imipenem to overcome class C β-lactamase mediated resistance. Although some analogs were more potent inhibitors of AmpC, none exhibited better synergy with imipenem than 1.

PubMed: 21676616
DOI: 10.1016/j.bmcl.2011.05.065

Experimental method

X-RAY DIFFRACTION (1.65 Å)