6bav: Difference between revisions

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 ==Crystal Structure of GltPh R397C in complex with S-Benzyl-L-Cysteine==
-<StructureSection load='6bav' size='340' side='right' caption='[[6bav]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
+<StructureSection load='6bav' size='340' side='right'caption='[[6bav]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6bav]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BAV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BAV FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6bav]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pyrococcus_horikoshii_OT3 Pyrococcus horikoshii OT3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BAV FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCS:BENZYLCYSTEINE'>BCS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 3.7&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nww|2nww]], [[6bat|6bat]], [[6bau|6bau]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCS:BENZYLCYSTEINE'>BCS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=6bav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bav OCA], [http://pdbe.org/6bav PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bav RCSB], [http://www.ebi.ac.uk/pdbsum/6bav PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bav ProSAT]</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=6bav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bav OCA], [https://pdbe.org/6bav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bav RCSB], [https://www.ebi.ac.uk/pdbsum/6bav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bav ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/GLT_PYRHO GLT_PYRHO]] Sodium-dependent, high-affinity amino acid transporter that mediates aspartate uptake (PubMed:17435767, PubMed:19380583, PubMed:17230192, Ref.11). Has only very low glutamate transport activity (PubMed:19380583, PubMed:17230192). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions, resulting in electrogenic transport (PubMed:17435767, PubMed:19380583, Ref.11). Na(+) binding enhances the affinity for aspartate (PubMed:19380583, Ref.11). Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (PubMed:17435767). In contrast to mammalian homologs, transport does not depend on pH or K(+) ions (PubMed:19380583).<ref>PMID:17230192</ref> <ref>PMID:17435767</ref> <ref>PMID:19380583</ref> [PDB:4P19]
+[https://www.uniprot.org/uniprot/GLT_PYRHO GLT_PYRHO] Sodium-dependent, high-affinity amino acid transporter that mediates aspartate uptake (PubMed:17435767, PubMed:19380583, PubMed:17230192, Ref.11). Has only very low glutamate transport activity (PubMed:19380583, PubMed:17230192). Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions, resulting in electrogenic transport (PubMed:17435767, PubMed:19380583, Ref.11). Na(+) binding enhances the affinity for aspartate (PubMed:19380583, Ref.11). Mediates Cl(-) flux that is not coupled to amino acid transport; this avoids the accumulation of negative charges due to aspartate and Na(+) symport (PubMed:17435767). In contrast to mammalian homologs, transport does not depend on pH or K(+) ions (PubMed:19380583).<ref>PMID:17230192</ref> <ref>PMID:17435767</ref> <ref>PMID:19380583</ref> [PDB:4P19]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 6bav" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Symporter 3D structures|Symporter 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Boudker, O]]
+[[Category: Large Structures]]
-[[Category: Font, J]]
+[[Category: Pyrococcus horikoshii OT3]]
-[[Category: Ryan, R M]]
+[[Category: Boudker O]]
-[[Category: Scopelliti, A J]]
+[[Category: Font J]]
-[[Category: Vandenberg, R J]]
+[[Category: Ryan RM]]
-[[Category: Amino acid transporter]]
+[[Category: Scopelliti AJ]]
-[[Category: Transmembrane transporter aspartate transporter]]
+[[Category: Vandenberg RJ]]
-[[Category: Transport protein]]