6ctc: Difference between revisions

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 ==Crystal structure of human transferrin bound to Triferic FPC iron pyrophosphate==
-<StructureSection load='6ctc' size='340' side='right' caption='[[6ctc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+<StructureSection load='6ctc' size='340' side='right'caption='[[6ctc]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6ctc]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CTC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CTC FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6ctc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CTC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CTC FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</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]] 2.6&#8491;</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=6ctc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ctc OCA], [http://pdbe.org/6ctc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ctc RCSB], [http://www.ebi.ac.uk/pdbsum/6ctc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ctc ProSAT]</span></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CO3:CARBONATE+ION'>CO3</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></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=6ctc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ctc OCA], [https://pdbe.org/6ctc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ctc RCSB], [https://www.ebi.ac.uk/pdbsum/6ctc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ctc ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[http://omim.org/entry/209300 209300]]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref> <ref>PMID:15466165</ref>
+[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN] Defects in TF are the cause of atransferrinemia (ATRAF) [MIM:[https://omim.org/entry/209300 209300]. Atransferrinemia is rare autosomal recessive disorder characterized by iron overload and hypochromic anemia.<ref>PMID:11110675</ref> <ref>PMID:15466165</ref>
 == Function ==
-[[http://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
+[https://www.uniprot.org/uniprot/TRFE_HUMAN TRFE_HUMAN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 21: @@
 </div>
 <div class="pdbe-citations 6ctc" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Transferrin 3D structures|Transferrin 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Edwards, T E]]
+[[Category: Homo sapiens]]
-[[Category: Pratt, R]]
+[[Category: Large Structures]]
-[[Category: Blood]]
+[[Category: Edwards TE]]
-[[Category: Fpc]]
+[[Category: Pratt R]]
-[[Category: Iron]]
-[[Category: Metal transport]]
-[[Category: Plasma]]
-[[Category: Pyrophosphate]]
-[[Category: Transferrin]]
-[[Category: Transfusion]]
-[[Category: Triferic iron]]