9BZN
High resolution structure of class A Beta-lactamase from Bordetella bronchiseptica RB50
Summary for 9BZN
| Entry DOI | 10.2210/pdb9bzn/pdb |
| Descriptor | class A Beta-lactamase, PenP superfamily, FORMIC ACID, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | lactamase, serine hydrolase, penp, csbid, center for structural biology of infectious diseases, structural genomics, hydrolase |
| Biological source | Bordetella bronchiseptica RB50 |
| Total number of polymer chains | 1 |
| Total formula weight | 29056.55 |
| Authors | Maltseva, N.,Kim, Y.,Endres, M.,Joachimiak, A.,Center for Structural Biology of Infectious Diseases (CSBID) (deposition date: 2024-05-24, release date: 2024-06-12, Last modification date: 2025-09-24) |
| Primary citation | Inniss, N.L.,Minasov, G.,Chang, C.,Tan, K.,Kim, Y.,Maltseva, N.,Stogios, P.,Filippova, E.,Michalska, K.,Osipiuk, J.,Jaroszewki, L.,Godzik, A.,Savchenko, A.,Joachimiak, A.,Anderson, W.F.,Satchell, K.J.F. Structural genomics of bacterial drug targets: Application of a high-throughput pipeline to solve 58 protein structures from pathogenic and related bacteria. Microbiol Resour Announc, 14:e0020025-e0020025, 2025 Cited by PubMed Abstract: Antibiotic resistance remains a leading cause of severe infections worldwide. Small changes in protein sequence can impact antibiotic efficacy. Here, we report deposition of 58 X-ray crystal structures of bacterial proteins that are known targets for antibiotics, which expands knowledge of structural variation to support future antibiotic discovery or modifications. PubMed: 40391899DOI: 10.1128/mra.00200-25 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.05 Å) |
Structure validation
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