Published May 20, 2021
| Version v1
Journal article
Open
The role of conserved residues in the DEDDh motif: the proton transfer mechanism of HIV-1 RNase H
Authors/Creators
- 1. Unversity of Konstanz, Department of Chemistry, King's College London, London, SE1 1DB, United Kingdom
- 2. Department of Chemistry, King's College London, London, SE1 1DB, United Kingdom
- 3. Department of Physics and Astronomy, University College London; London WC1E 6BT, United Kingdom
- 4. Universoty of Konstanz
- 5. Department of Chemistry and Biochemistry, University of Oklahoma, 101 Stephenson Parkway, Norman, OK 73019–5251, USA
- 6. Department of Chemistry, King's College London, London, SE1 1DB, United Kingdom, Department of Physics and Astronomy, University College London; London WC1E 6BT, United Kingdom
Description
Supplemental information containing
- PyMol session of aligned structures for Figure 6
- PyMol session of aligned metal ion binding sites for site F, C from MD simulation of HIV-1 RNase H, crystal of 2NUG and crystal of BhRNase H 600 sec 6DOG
- QM/MM geometries (slightly edited to get consistent bonds, no changed coordinates)
- Source code of interactive figure
Files
README.md
Files
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Additional details
Related works
- Is supplement to
- Journal article: 10.1021/acscatal.1c01493 (DOI)