4v81: Difference between revisions

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== Structural highlights ==

<table><tr><td colspan='2'>[[4v81]] is a 32 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae~~]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3p9d 3p9d] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3p9e 3p9e~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V81 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V81 FirstGlance]. <br>

<table><tr><td colspan='2'>[[4v81]] is a 32 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V81 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V81 FirstGlance]. <br>

</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8Å</td></tr>

<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

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</table>

== Function ==

[https://www.uniprot.org/uniprot/~~TCPA_YEAST TCPA_YEAST~~] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.

[https://www.uniprot.org/uniprot/TCPZ_YEAST TCPZ_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.

== Publication Abstract from PubMed ==

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 <StructureSection load='4v81' size='340' side='right'caption='[[4v81]], [[Resolution|resolution]] 3.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4v81]] is a 32 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3p9d 3p9d] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3p9e 3p9e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V81 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V81 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4v81]] is a 32 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V81 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V81 FirstGlance]. <br>
 </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8&#8491;</td></tr>
 <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=BEF:BERYLLIUM+TRIFLUORIDE+ION'>BEF</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/TCPA_YEAST TCPA_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.
+[https://www.uniprot.org/uniprot/TCPZ_YEAST TCPZ_YEAST] Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==