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-Structure paper
Title | Arginine residues at internal positions in a protein are always charged. |
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Journal, issue, pages | Proc. Natl. Acad. Sci. USA, Vol. 108, Page 18954-18959, Year 2011 |
Publish date | May 15, 2008 (structure data deposition date) |
![]() | Harms, M.J. / Schlessman, J.L. / Sue, G.R. / Garcia-Moreno E, B. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 1.9 - 2.15 Å |
Structure data | ![]() PDB-3d4w: ![]() PDB-3d8g: ![]() PDB-3dhq: |
Chemicals | ![]() ChemComp-PO4: ![]() ChemComp-MPD: ![]() ChemComp-HOH: ![]() ChemComp-CA: ![]() ChemComp-THP: |
Source |
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![]() | HYDROLASE / Staphylococcal nuclease / hyperstable variant / internal arg / Endonuclease / Metal-binding / Secreted / Zymogen / Nuclease / Membrane |