3AGI
High resolution X-ray analysis of Arg-lysozyme complex in the presence of 500 mM Arg
Summary for 3AGI
Entry DOI | 10.2210/pdb3agi/pdb |
Related | 3A34 3AGG 3AGH |
Descriptor | Lysozyme C, ACETATE ION, ARGININE, ... (6 entities in total) |
Functional Keywords | hydrolase, lysozyme, glycosidase, arginine, allergen, antimicrobial, bacteriolytic enzyme, disulfide bond |
Biological source | Gallus gallus (chicken) |
Cellular location | Secreted: P00698 |
Total number of polymer chains | 1 |
Total formula weight | 15222.44 |
Authors | Ito, L.,Shiraki, K.,Hasegawa, K.,Baba, S.,Kumasaka, T. (deposition date: 2010-03-31, release date: 2011-03-23, Last modification date: 2023-11-01) |
Primary citation | Ito, L.,Shiraki, K.,Matsuura, T.,Okumura, M.,Hasegawa, K.,Baba, S.,Yamaguchi, H.,Kumasaka, T. High-resolution X-ray analysis reveals binding of arginine to aromatic residues of lysozyme surface: implication of suppression of protein aggregation by arginine Protein Eng.Des.Sel., 24:269-274, 2011 Cited by PubMed: 21084280DOI: 10.1093/protein/gzq101 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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