8I1W
The asymmetric structure of homodimeric E. coli TrpRS bound with tryptophanyl adenylate at one of its two active pockets
Summary for 8I1W
Entry DOI | 10.2210/pdb8i1w/pdb |
Descriptor | Tryptophan--tRNA ligase, SULFATE ION, TRYPTOPHANYL-5'AMP, ... (4 entities in total) |
Functional Keywords | homodimer, asymmetric conformation, intermediate product, half-of-the-sites reactivity, aminoacyl-trna synthetase, ligase |
Biological source | Escherichia coli K-12 |
Total number of polymer chains | 2 |
Total formula weight | 77665.16 |
Authors | |
Primary citation | Xiang, M.,Xia, K.,Chen, B.,Luo, Z.,Yu, Y.,Jiang, L.,Zhou, H. An asymmetric structure of bacterial TrpRS supports the half-of-the-sites catalytic mechanism and facilitates antimicrobial screening. Nucleic Acids Res., 51:4637-4649, 2023 Cited by PubMed: 37070195DOI: 10.1093/nar/gkad278 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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