3ba6
From Proteopedia
(Difference between revisions)
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<StructureSection load='3ba6' size='340' side='right'caption='[[3ba6]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='3ba6' size='340' side='right'caption='[[3ba6]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3ba6]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3ba6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BA6 FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AN2:AMP+PHOSPHORAMIDATE'>AN2</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AN2:AMP+PHOSPHORAMIDATE'>AN2</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHD:ASPARTYL+PHOSPHATE'>PHD</scene></td></tr> | ||
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1t5s|1t5s]], [[1t5t|1t5t]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1t5s|1t5s]], [[1t5t|1t5t]]</div></td></tr> |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Calcium-transporting_ATPase Calcium-transporting ATPase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.3.8 3.6.3.8] </span></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ba6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ba6 OCA], [https://pdbe.org/3ba6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ba6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ba6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ba6 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[https://www.uniprot.org/uniprot/AT2A1_RABIT AT2A1_RABIT]] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity). |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] |
Revision as of 11:29, 5 January 2022
Structure of the Ca2E1P phosphoenzyme intermediate of the SERCA Ca2+-ATPase
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Categories: Calcium-transporting ATPase | Large Structures | Oryctolagus cuniculus | Gyrup, C | Moller, J V | Morth, J P | Nissen, P | Olesen, C | Oxvig, C | Picard, M | Winther, A M.L | Alternative splicing | Aspartyl-phosphoanhydride | Atp-binding | Calcium | Calcium transport | Endoplasmic reticulum | Hydrolase | Ion transport | Magnesium | Membrane protein | Metal-binding | Nucleotide-binding | P-type atpase | Phosphoenzyme | Phosphorylation | Sarcoplasmic reticulum | Transmembrane | Transport