5xdo

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Current revision (08:00, 22 November 2023) (edit) (undo)
 
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<StructureSection load='5xdo' size='340' side='right'caption='[[5xdo]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
<StructureSection load='5xdo' size='340' side='right'caption='[[5xdo]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xdo]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XDO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XDO FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xdo]] is a 2 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=5XDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XDO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEX:HEXANE'>HEX</scene>, <scene name='pdbligand=LNK:PENTANE'>LNK</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene></td></tr>
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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]] 3.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5xdn|5xdn]]</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=HEX:HEXANE'>HEX</scene>, <scene name='pdbligand=LNK:PENTANE'>LNK</scene>, <scene name='pdbligand=OCT:N-OCTANE'>OCT</scene>, <scene name='pdbligand=SPD:SPERMIDINE'>SPD</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xdo OCA], [http://pdbe.org/5xdo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xdo RCSB], [http://www.ebi.ac.uk/pdbsum/5xdo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xdo ProSAT]</span></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=5xdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xdo OCA], [https://pdbe.org/5xdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xdo RCSB], [https://www.ebi.ac.uk/pdbsum/5xdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xdo ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/VDAC1_HUMAN VDAC1_HUMAN]] Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.<ref>PMID:11845315</ref> <ref>PMID:15033708</ref> <ref>PMID:18755977</ref>
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[https://www.uniprot.org/uniprot/VDAC1_HUMAN VDAC1_HUMAN] Forms a channel through the mitochondrial outer membrane and also the plasma membrane. The channel at the outer mitochondrial membrane allows diffusion of small hydrophilic molecules; in the plasma membrane it is involved in cell volume regulation and apoptosis. It adopts an open conformation at low or zero membrane potential and a closed conformation at potentials above 30-40 mV. The open state has a weak anion selectivity whereas the closed state is cation-selective. May participate in the formation of the permeability transition pore complex (PTPC) responsible for the release of mitochondrial products that triggers apoptosis.<ref>PMID:11845315</ref> <ref>PMID:15033708</ref> <ref>PMID:18755977</ref>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hosaka, T]]
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[[Category: Hosaka T]]
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[[Category: Kimura-Someya, T]]
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[[Category: Kimura-Someya T]]
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[[Category: Shirouzu, M]]
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[[Category: Shirouzu M]]
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[[Category: Beta-barrel structure]]
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[[Category: Cell-free synthesis]]
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[[Category: Membrane protein]]
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Current revision

Crystal structure of human voltage-dependent anion channel 1 (hVDAC1) in C222 space group

PDB ID 5xdo

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