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-Structure paper
Title | Cyclopiazonic acid is complexed to a divalent metal ion when bound to the sarcoplasmic reticulum Ca2+-ATPase. |
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Journal, issue, pages | J. Biol. Chem., Year 2009 |
Publish date | Dec 8, 2008 (structure data deposition date) |
![]() | Laursen, M. / Bublitz, M. / Moncoq, K. / Olesen, C. / Moeller, J.V. / Young, H.S. / Nissen, P. / Morth, J.P. |
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Methods | X-ray diffraction |
Resolution | 2.5 - 3.2 Å |
Structure data | ![]() PDB-3fgo: ![]() PDB-3fpb: ![]() PDB-3fps: |
Chemicals | ![]() ChemComp-MG: ![]() ChemComp-MF4: ![]() ChemComp-K: ![]() ChemComp-CZA: ![]() ChemComp-MN: ![]() ChemComp-ACP: ![]() ChemComp-ACT: ![]() ChemComp-HOH: ![]() ChemComp-ATP: ![]() ChemComp-ADP: |
Source |
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![]() | HYDROLASE / Calcium pump / SERCA / nonhydrolyzable ATP analog / P-Type-ATPase / phosphorylation / cyclopiazonic acid / CPA / Alternative splicing / ATP-binding / Calcium / Calcium transport / Endoplasmic reticulum / Ion transport / Magnesium / Membrane / Metal-binding / Nucleotide-binding / Phosphoprotein / Sarcoplasmic reticulum / Transmembrane / Transport / P-TYPE ATPase / CALCIUM-TRANSPORTING ATPASE SARCOPLASMIC RETICULUM / FAST TWITCH SKELETAL MUSCLE ISOFORM |