5EOP
Crystal structure of human Angiogenin at 1.35 Angstroms resolution
Summary for 5EOP
| Entry DOI | 10.2210/pdb5eop/pdb |
| Descriptor | Angiogenin (2 entities in total) |
| Functional Keywords | hydrolase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Cytoplasmic vesicle, secretory vesicle lumen : P03950 |
| Total number of polymer chains | 1 |
| Total formula weight | 13943.79 |
| Authors | Chatzileontiadou, D.S.M.,Tsirkone, V.G.,Dossi, K.,Leonidas, D.D. (deposition date: 2015-11-10, release date: 2016-08-17, Last modification date: 2024-01-10) |
| Primary citation | Chatzileontiadou, D.S.,Tsirkone, V.G.,Dossi, K.,Kassouni, A.G.,Liggri, P.G.,Kantsadi, A.L.,Stravodimos, G.A.,Balatsos, N.A.,Skamnaki, V.T.,Leonidas, D.D. The ammonium sulfate inhibition of human angiogenin. Febs Lett., 590:3005-3018, 2016 Cited by PubMed Abstract: In this study, we investigate the inhibition of human angiogenin by ammonium sulfate. The inhibitory potency of ammonium sulfate for human angiogenin (IC50 = 123.5 ± 14.9 mm) is comparable to that previously reported for RNase A (119.0 ± 6.5 mm) and RNase 2 (95.7 ± 9.3 mm). However, analysis of two X-ray crystal structures of human angiogenin in complex with sulfate anions (in acidic and basic pH environments, respectively) indicates an entirely distinct mechanism of inhibition. While ammonium sulfate inhibits the ribonucleolytic activity of RNase A and RNase 2 by binding to the active site of these enzymes, sulfate anions bind only to peripheral substrate anion-binding subsites of human angiogenin, and not to the active site. PubMed: 27483019DOI: 10.1002/1873-3468.12335 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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