This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1vpx

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (14:53, 20 September 2023) (edit) (undo)
 
(One intermediate revision not shown.)
Line 3: Line 3:
<StructureSection load='1vpx' size='340' side='right'caption='[[1vpx]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
<StructureSection load='1vpx' size='340' side='right'caption='[[1vpx]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[1vpx]] is a 20 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VPX OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1VPX FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[1vpx]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VPX FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM0295 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Transaldolase Transaldolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.2.1.2 2.2.1.2] </span></td></tr>
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1vpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vpx OCA], [https://pdbe.org/1vpx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vpx RCSB], [https://www.ebi.ac.uk/pdbsum/1vpx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vpx ProSAT], [https://www.topsan.org/Proteins/JCSG/1vpx TOPSAN]</span></td></tr>
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1vpx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vpx OCA], [http://pdbe.org/1vpx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1vpx RCSB], [http://www.ebi.ac.uk/pdbsum/1vpx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1vpx ProSAT], [http://www.topsan.org/Proteins/JCSG/1vpx TOPSAN]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/TAL_THEMA TAL_THEMA]] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
+
[https://www.uniprot.org/uniprot/TAL_THEMA TAL_THEMA] Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Line 23: Line 22:
==See Also==
==See Also==
-
*[[Transaldolase|Transaldolase]]
+
*[[Transaldolase 3D structures|Transaldolase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Atcc 43589]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Transaldolase]]
+
[[Category: Thermotoga maritima]]
-
[[Category: Structural genomic]]
+
-
[[Category: Jcsg]]
+
-
[[Category: PSI, Protein structure initiative]]
+
-
[[Category: Tm0295]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal structure of Transaldolase (EC 2.2.1.2) (TM0295) from Thermotoga maritima at 2.40 A resolution

PDB ID 1vpx

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools