9JWD
Crystal structure of RNAs A treated with sodium cyanide
Summary for 9JWD
Entry DOI | 10.2210/pdb9jwd/pdb |
Descriptor | Ribonuclease pancreatic, CYANIDE ION, GLYCEROL, ... (6 entities in total) |
Functional Keywords | hydrolase |
Biological source | Bos taurus (domestic cattle) |
Total number of polymer chains | 1 |
Total formula weight | 14028.86 |
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 (2.22 Å) |
Structure validation
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