5TY0
2.22 Angstrom Crystal Structure of N-terminal Fragment (residues 1-419) of Elongation Factor G from Legionella pneumophila.
Summary for 5TY0
| Entry DOI | 10.2210/pdb5ty0/pdb |
| Descriptor | Elongation factor G, SODIUM ION, beta-D-glucopyranose, ... (4 entities in total) |
| Functional Keywords | structural genomics, center for structural genomics of infectious diseases, csgid, elongation factor g, lipid-binding protein, lipid binding protein |
| Biological source | Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513) |
| Cellular location | Cytoplasm : Q5ZYP6 |
| Total number of polymer chains | 1 |
| Total formula weight | 47232.70 |
| Authors | Minasov, G.,Wawrzak, Z.,Shuvalova, L.,Cardona-Correa, A.,Dubrovska, I.,Grimshaw, S.,Kwon, K.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2016-11-17, release date: 2016-11-30, Last modification date: 2026-02-11) |
| 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 (2.22 Å) |
Structure validation
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