9JWH
Crystal structure of native bovine pancreatic RNAs A
Summary for 9JWH
Entry DOI | 10.2210/pdb9jwh/pdb |
Descriptor | Ribonuclease pancreatic, CHLORIDE ION, SULFATE ION, ... (4 entities in total) |
Functional Keywords | hydrolase |
Biological source | Bos taurus (domestic cattle) |
Total number of polymer chains | 1 |
Total formula weight | 14042.26 |
Authors | |
Primary citation | Shah, N.,Akbar, Z.,Ahmad, M.S. Cyanide mediated conformational changes resulted in the displacement of sulfate ion from the active site of bovine pancreatic ribonuclease A. Biochem.Biophys.Res.Commun., 736:150868-150868, 2024 Cited by PubMed Abstract: Ribonuclease A is a major hydrolyzing enzyme involved in the hydrolysis of RNA. The crystals of bovine pancreatic RNase A (bpRNase A) were grown at pH 5.5. The effect of sodium cyanide on bpRNase A was assessed by adding it directly to the crystal containing well. Treating the crystals of bpRNase A with sodium cyanide resulted in the displacement of the sulfate ion from the active site of bpRNase A, while the additional sulfate ion, bound to Ala-4, remained unaffected. The addition of sodium cyanide to bpRNase A crystals did not show change in the secondary structure elements of the enzyme. This study was conducted to check the effect of cyanide on bpRNase A crystals and to displace sulfate ion from its active site. PubMed: 39490154DOI: 10.1016/j.bbrc.2024.150868 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
Download full validation report
