6MLA
Crystal structure of the periplasmic Lysine-, Arginine-, Ornithine-binding protein (LAO) D161A mutant from Salmonella typhimurium complexed with arginine
Summary for 6MLA
Entry DOI | 10.2210/pdb6mla/pdb |
Related | 6MKU 6MKW 6MKX 6ML0 6ML9 |
Descriptor | Lysine/arginine/ornithine-binding periplasmic protein, ARGININE, ACETATE ION, ... (6 entities in total) |
Functional Keywords | periplasmic binding protein, lao, thermodynamics, protein ligand complex, protein binding |
Biological source | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
Total number of polymer chains | 1 |
Total formula weight | 26435.62 |
Authors | Romero-Romero, S.,Vergara, R.,Espinoza-Perez, G.,Rodriguez-Romero, A. (deposition date: 2018-09-27, release date: 2019-08-07, Last modification date: 2023-10-11) |
Primary citation | Vergara, R.,Romero-Romero, S.,Velazquez-Lopez, I.,Espinoza-Perez, G.,Rodriguez-Hernandez, A.,Pulido, N.O.,Sosa-Peinado, A.,Rodriguez-Romero, A.,Fernandez-Velasco, D.A. The interplay of protein-ligand and water-mediated interactions shape affinity and selectivity in the LAO binding protein. Febs J., 287:763-782, 2020 Cited by PubMed: 31348608DOI: 10.1111/febs.15019 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.582 Å) |
Structure validation
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