9GYH
HEW Lysozyme with His 15 functionalized with iodoacetamide
This is a non-PDB format compatible entry.
Summary for 9GYH
| Entry DOI | 10.2210/pdb9gyh/pdb |
| Related | 7a70 |
| Descriptor | Lysozyme C, SODIUM ION, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | hew lysozime, iodoacetamide, functionalized histidine, hydrolase |
| Biological source | Gallus gallus (chicken) |
| Total number of polymer chains | 2 |
| Total formula weight | 29104.01 |
| Authors | da Silva, J.S.P.,Delgado, J.M.L.,Bruno, F.,Calderone, V.,Ravera, E. (deposition date: 2024-10-02, release date: 2025-02-26) |
| Primary citation | Malanho da Silva, J.,Lanuza, J.,Bruno, F.,Calderone, V.,Ravera, E. The structure of His15 acetamide-modified hen egg-white lysozyme: a nice surprise from an old friend. Acta Crystallogr.,Sect.F, 81:41-46, 2025 Cited by PubMed Abstract: Hen egg-white lysozyme (HEWL) is a small polycationic protein which is highly soluble and stable. This has led to it becoming a `molecular laboratory' where chemical biological operations and structural techniques are tested. To date, HEWL accounts for 1233 PDB entries, roughly 0.5% of the total, making it the best-represented protein in the PDB. With the aim of unambiguously identifying the N atom of the His15 side chain that is most reactive towards iodoacetamide, the structure of chemically modified HEWL was determined by crystallizing it using the `15 minutes lysozyme' protocol. This protocol invariably yields tetragonal crystals of the unmodified protein. To our surprise, we found that the crystals of the modified protein had similar unit-cell parameters but that refinement was only possible when considering an orthorhombic system. PubMed: 39804568DOI: 10.1107/S2053230X2500010X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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