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4c3z

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'''Unreleased structure'''
 
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The entry 4c3z is ON HOLD until Paper Publication
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==Nucleotide-free crystal structure of nucleotide-binding domain 1 from human MRP1 supports a general-base catalysis mechanism for ATP hydrolysis.==
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<StructureSection load='4c3z' size='340' side='right'caption='[[4c3z]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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Authors: Chaptal, V., GueguenChaignon, V., Magnard, S., Falson, P., DiPietro, A., BaubichonCortay, H.
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4c3z]] 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=4C3Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C3Z FirstGlance]. <br>
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Description: Nucleotide-free crystal structure of nucleotide-binding domain 1 from human MRP1 supports a general-base catalysis mechanism for ATP hydrolysis.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c3z OCA], [https://pdbe.org/4c3z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c3z RCSB], [https://www.ebi.ac.uk/pdbsum/4c3z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c3z ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MRP1_HUMAN MRP1_HUMAN] Mediates export of organic anions and drugs from the cytoplasm. Mediates ATP-dependent transport of glutathione and glutathione conjugates, leukotriene C4, estradiol-17-beta-o-glucuronide, methotrexate, antiviral drugs and other xenobiotics. Confers resistance to anticancer drugs. Hydrolyzes ATP with low efficiency.<ref>PMID:10064732</ref> <ref>PMID:11114332</ref> <ref>PMID:16230346</ref>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Baubichon-Cortay H]]
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[[Category: Chaptal V]]
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[[Category: Di Pietro A]]
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[[Category: Falson P]]
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[[Category: Gueguen-Chaignon V]]
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[[Category: Magnard S]]

Current revision

Nucleotide-free crystal structure of nucleotide-binding domain 1 from human MRP1 supports a general-base catalysis mechanism for ATP hydrolysis.

PDB ID 4c3z

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