8fhk
From Proteopedia
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- | '''Unreleased structure''' | ||
- | + | ==Heterodimeric ABC transporter BmrCD in the occluded conformation bound to ATP: BmrCD_OC-ATP== | |
- | + | <StructureSection load='8fhk' size='340' side='right'caption='[[8fhk]], [[Resolution|resolution]] 2.90Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[8fhk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8FHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8FHK FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9Å</td></tr> | |
- | [[Category: | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POV:(2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>POV</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=8fhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8fhk OCA], [https://pdbe.org/8fhk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8fhk RCSB], [https://www.ebi.ac.uk/pdbsum/8fhk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8fhk ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/YHEH_BACSU YHEH_BACSU] Involved in the transport of four structurally unrelated drugs, including doxorubicin and mitoxantrone. Transmembrane domains (TMD) form a pore in the membrane and the ATP-binding domain (NBD) is responsible for energy generation.<ref>PMID:19167342</ref> | ||
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Mchaourab H]] | ||
+ | [[Category: Tang Q]] |
Current revision
Heterodimeric ABC transporter BmrCD in the occluded conformation bound to ATP: BmrCD_OC-ATP
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