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3ldl
From Proteopedia
(Difference between revisions)
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==Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with ATP== | ==Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with ATP== | ||
<StructureSection load='3ldl' size='340' side='right' caption='[[3ldl]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='3ldl' size='340' side='right' caption='[[3ldl]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3ldl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3ldl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LDL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3LDL FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ldn|3ldn]], [[3ldo|3ldo]], [[3ldp|3ldp]], [[3ldq|3ldq]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ldn|3ldn]], [[3ldo|3ldo]], [[3ldp|3ldp]], [[3ldq|3ldq]]</td></tr> | ||
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSPA5, GRP78 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HSPA5, GRP78 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ldl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ldl OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ldl RCSB], [http://www.ebi.ac.uk/pdbsum/3ldl PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ldl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ldl OCA], [http://pdbe.org/3ldl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ldl RCSB], [http://www.ebi.ac.uk/pdbsum/3ldl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ldl ProSAT]</span></td></tr> |
</table> | </table> | ||
== Disease == | == Disease == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 3ldl" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Human]] |
[[Category: Dokurno, P]] | [[Category: Dokurno, P]] | ||
[[Category: Macias, A T]] | [[Category: Macias, A T]] | ||
Revision as of 20:39, 4 August 2016
Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with ATP
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Categories: Human | Dokurno, P | Macias, A T | Massey, A J | Shaw, T | Surgenor, A E | Williamson, D S | Adenosine | Atp-binding | Chaperone | Endoplasmic reticulum | Grp78 | Heat shock | Hsc70 | Hsp70 | Nucleoside | Nucleotide-binding | Phosphoprotein | Protein folding | Selectivity | Small molecule inhibitor | Stress response
