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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) |
Authors | Prats-Ejarque, G. / Blanco, J.A. / Salazar, V.A. / Nogues, V.M. / Moussaoui, M. / Boix, E. |
External links | Biochim Biophys Acta Gen Subj / PubMed:30287244 |
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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Keywords | HYDROLASE / RNase A / p2 subsite / exonuclease activity / RNASE K6 / PANCREATIC RIBONUCLEASE / Ribonuclease A / 3'-CMP / mononucleotide inhibitor / high resolution |