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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) |
Authors | Srivastava, S.K. / Rajasree, K. / Gopal, B. |
External links | Biochim. Biophys. Acta / PubMed:21745603 |
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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Keywords | 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 |