5V0I
Crystal Structure of Tryptophanyl-tRNA Synthetase from Escherichia coli Complexed with AMP and Tryptophan
Summary for 5V0I
| Entry DOI | 10.2210/pdb5v0i/pdb |
| Descriptor | Tryptophan--tRNA ligase, ADENOSINE MONOPHOSPHATE, TRYPTOPHAN, ... (5 entities in total) |
| Functional Keywords | csgid, tryptophanyl-trna synthetase, a/b sandwich, structural genomics, center for structural genomics of infectious diseases, ligase |
| Biological source | Escherichia coli O157:H7 str. EDL933 |
| Total number of polymer chains | 2 |
| Total formula weight | 76773.03 |
| Authors | Maltseva, N.,Kim, Y.,Mulligan, R.,Grimshaw, S.G.,Joachimiak, A.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2017-02-28, release date: 2017-03-22, Last modification date: 2026-03-25) |
| 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 (1.9 Å) |
Structure validation
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