6XKS
Crystal structure of domain A from the periplasmic Lysine-, Arginine-, Ornithine-binding protein (LAO) of Salmonella typhimurium
Summary for 6XKS
Entry DOI | 10.2210/pdb6xks/pdb |
Descriptor | Histidine ABC transporter substrate-binding protein HisJ, ACETATE ION, DI(HYDROXYETHYL)ETHER, ... (4 entities in total) |
Functional Keywords | periplasmic binding protein, lao, protein folding, thermodynamics, kinetics, protein binding |
Biological source | Salmonella typhimurium More |
Total number of polymer chains | 3 |
Total formula weight | 49077.55 |
Authors | Romero-Romero, S.,Berrocal, T.,Vergara, R.,Espinoza-Perez, G.,Rodriguez-Romero, A. (deposition date: 2020-06-27, release date: 2021-07-14, Last modification date: 2023-10-25) |
Primary citation | Vergara, R.,Berrocal, T.,Juarez Mejia, E.I.,Romero-Romero, S.,Velazquez-Lopez, I.,Pulido, N.O.,Lopez Sanchez, H.A.,Silva, D.A.,Costas, M.,Rodriguez-Romero, A.,Rodriguez-Sotres, R.,Sosa-Peinado, A.,Fernandez-Velasco, D.A. Thermodynamic and kinetic analysis of the LAO binding protein and its isolated domains reveal non-additivity in stability, folding and function. Febs J., 2023 Cited by PubMed: 37178351DOI: 10.1111/febs.16819 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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