9rtb: Difference between revisions
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New page: '''Unreleased structure''' The entry 9rtb is ON HOLD Authors: Paolillo, M., Ferraro, G., Banneville, A.S., Cornaciu, I., Pica, A., Merlino, A. Description: Crystal structure of the add... |
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==Crystal structure of the adduct formed upon reaction of [V(IV)O(acetylacetonate)2] with human serum transferrin with Fe(III) bound at the C-lobe only== | |||
<StructureSection load='9rtb' size='340' side='right'caption='[[9rtb]], [[Resolution|resolution]] 1.93Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9rtb]] 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=9RTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9RTB 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]] 1.93Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1JJT:bis(oxidanyl)-oxidanylidene-(oxidanyl(oxidanylidene)vanadio)oxy-vanadium'>A1JJT</scene>, <scene name='pdbligand=BCT:BICARBONATE+ION'>BCT</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> | ||
[[Category: | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9rtb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9rtb OCA], [https://pdbe.org/9rtb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9rtb RCSB], [https://www.ebi.ac.uk/pdbsum/9rtb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9rtb ProSAT]</span></td></tr> | ||
[[Category: | </table> | ||
[[Category: | == Disease == | ||
[[Category: Ferraro | [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> | ||
[[Category: | == Function == | ||
[[Category: | [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. | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Banneville AS]] | |||
[[Category: Cornaciu I]] | |||
[[Category: Ferraro G]] | |||
[[Category: Merlino A]] | |||
[[Category: Paolillo M]] | |||
[[Category: Pica A]] | |||
Latest revision as of 07:06, 15 July 2026
Crystal structure of the adduct formed upon reaction of [V(IV)O(acetylacetonate)2] with human serum transferrin with Fe(III) bound at the C-lobe only
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