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==NMR Structure of protoporphyrin-IX bound murine p22HBP== | ==NMR Structure of protoporphyrin-IX bound murine p22HBP== | ||
<StructureSection load='4a1m' size='340' side='right' caption='[[4a1m]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='4a1m' size='340' side='right'caption='[[4a1m]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4a1m]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4a1m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4A1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4A1M FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2gov|2gov]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2gov|2gov]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4a1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4a1m OCA], [https://pdbe.org/4a1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4a1m RCSB], [https://www.ebi.ac.uk/pdbsum/4a1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4a1m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/HEBP1_MOUSE HEBP1_MOUSE]] May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities.<ref>PMID:12413491</ref> <ref>PMID:16905545</ref> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Lk3 transgenic mice]] | [[Category: Lk3 transgenic mice]] | ||
[[Category: Dias, J S]] | [[Category: Dias, J S]] |
Revision as of 10:38, 18 August 2022
NMR Structure of protoporphyrin-IX bound murine p22HBPNMR Structure of protoporphyrin-IX bound murine p22HBP
Structural highlights
Function[HEBP1_MOUSE] May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities.[1] [2] References
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