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-Structure paper
Title | Characterization of an RNase with two catalytic centers. Human RNase6 catalytic and phosphate-binding site arrangement favors the endonuclease cleavage of polymeric substrates. |
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Journal, issue, pages | Biochim Biophys Acta Gen Subj, Vol. 1863, Page 105-117, Year 2019 |
Publish date | Nov 17, 2015 (structure data deposition date) |
![]() | Prats-Ejarque, G. / Blanco, J.A. / Salazar, V.A. / Nogues, V.M. / Moussaoui, M. / Boix, E. |
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Methods | X-ray diffraction |
Resolution | 1.042 - 2.1 Å |
Structure data | ![]() PDB-5et4: ![]() PDB-5oab: ![]() PDB-5ogh: ![]() PDB-6enp: |
Chemicals | ![]() ChemComp-C3P: ![]() ChemComp-MPD: ![]() ChemComp-HOH: ![]() ChemComp-PO4: ![]() ChemComp-NA: ![]() ChemComp-CL: ![]() ChemComp-K: ![]() ChemComp-SO4: ![]() ChemComp-ZN: |
Source |
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![]() | HYDROLASE / RNase A / p2 subsite / exonuclease activity / RNASE K6 / PANCREATIC RIBONUCLEASE / Ribonuclease A / 3'-CMP / mononucleotide inhibitor / high resolution |