1B5X
Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and x-ray analysis of six ser->ala mutants
Summary for 1B5X
Entry DOI | 10.2210/pdb1b5x/pdb |
Descriptor | PROTEIN (LYSOZYME), SODIUM ION (3 entities in total) |
Functional Keywords | hydrogen bond, stability, hydrolase |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: P61626 |
Total number of polymer chains | 1 |
Total formula weight | 14727.68 |
Authors | Takano, K.,Yamagata, Y.,Kubota, M.,Funahashi, J.,Fujii, S.,Yutani, K. (deposition date: 1999-01-11, release date: 1999-01-20, Last modification date: 2024-04-03) |
Primary citation | Takano, K.,Yamagata, Y.,Kubota, M.,Funahashi, J.,Fujii, S.,Yutani, K. Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants. Biochemistry, 38:6623-6629, 1999 Cited by PubMed: 10350481DOI: 10.1021/bi9901228 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
Download full validation report