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-Structure paper
Title | The structure of an unconventional HD-GYP protein from Bdellovibrio reveals the roles of conserved residues in this class of cyclic-di-GMP phosphodiesterases. |
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Journal, issue, pages | MBio, Vol. 2, Year 2011 |
Publish date | Aug 31, 2011 (structure data deposition date) |
![]() | Lovering, A.L. / Capeness, M.J. / Lambert, C. / Hobley, L. / Sockett, R.E. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 1.28 - 2.641 Å |
Structure data | ![]() PDB-3tm8: ![]() PDB-3tmb: ![]() PDB-3tmc: ![]() PDB-3tmd: |
Chemicals | ![]() ChemComp-PO4: ![]() ChemComp-FE: ![]() ChemComp-DMS: ![]() ChemComp-EDO: ![]() ChemComp-HOH: |
Source |
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![]() | HYDROLASE / SIGNALING PROTEIN / HD-GYP / phosphodiesterase / UNKNOWN FUNCTION |