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-Structure paper
Title | Conformational basis for substrate recognition and regulation of catalytic activity in Staphylococcus aureus nucleoside di-phosphate kinase. |
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Journal, issue, pages | Biochim. Biophys. Acta, Vol. 1814, Page 1349-1357, Year 2011 |
Publish date | Jan 6, 2011 (structure data deposition date) |
![]() | Srivastava, S.K. / Rajasree, K. / Gopal, B. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 2.22 - 2.9 Å |
Structure data | ![]() PDB-3q83: ![]() PDB-3q86: ![]() PDB-3q89: ![]() PDB-3q8u: ![]() PDB-3q8v: ![]() PDB-3q8y: |
Chemicals | ![]() ChemComp-HOH: ![]() ChemComp-GTP: ![]() ChemComp-MG: ![]() ChemComp-CDP: ![]() ChemComp-ADP: ![]() ChemComp-UDP: ![]() ChemComp-VO4: |
Source |
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![]() | TRANSFERASE / Ferridoxin fold / alpha-beta protein family / Nucleoside diphosphate kinases (NDKs) catalyze the transfer of a gamma phosphate from nucleoside triphosphates to nucleoside diphosphate / Nucleotide binding / Metal binding / Phosphorylation / Kinase / Nucleotide metabolism / Nucleoside diphosphate kinases (NDKs) / transfer / a gamma phosphate / nucleoside triphosphates / nucleoside diphosphate / Nucleotide binding Magnesium / Magnesium / gamma phosphate |