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2wu5
From Proteopedia
(Difference between revisions)
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<StructureSection load='2wu5' size='340' side='right'caption='[[2wu5]], [[Resolution|resolution]] 2.80Å' scene=''> | <StructureSection load='2wu5' size='340' side='right'caption='[[2wu5]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2wu5]] is a 12 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2wu5]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WU5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WU5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CBE:2-METHYL-N-PHENYL-5,6-DIHYDRO-1,4-OXATHIINE-3-CARBOXAMIDE'>CBE</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TEO:MALATE+LIKE+INTERMEDIATE'>TEO</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CBE:2-METHYL-N-PHENYL-5,6-DIHYDRO-1,4-OXATHIINE-3-CARBOXAMIDE'>CBE</scene>, <scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=TEO:MALATE+LIKE+INTERMEDIATE'>TEO</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wp9|2wp9]], [[2wdq|2wdq]], [[2wdr|2wdr]], [[1nen|1nen]], [[1nek|1nek]], [[2wu2|2wu2]], [[2acz|2acz]], [[2wdv|2wdv]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wp9|2wp9]], [[2wdq|2wdq]], [[2wdr|2wdr]], [[1nen|1nen]], [[1nek|1nek]], [[2wu2|2wu2]], [[2acz|2acz]], [[2wdv|2wdv]]</div></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Succinate_dehydrogenase_(quinone) Succinate dehydrogenase (quinone)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.5.1 1.3.5.1] </span></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=2wu5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wu5 OCA], [https://pdbe.org/2wu5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wu5 RCSB], [https://www.ebi.ac.uk/pdbsum/2wu5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wu5 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/DHSD_ECOLI DHSD_ECOLI]] Membrane-anchoring subunit of succinate dehydrogenase (SDH). [[https://www.uniprot.org/uniprot/DHSA_ECOLI DHSA_ECOLI]] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. [[https://www.uniprot.org/uniprot/DHSC_ECOLI DHSC_ECOLI]] Membrane-anchoring subunit of succinate dehydrogenase (SDH). [[https://www.uniprot.org/uniprot/DHSB_ECOLI DHSB_ECOLI]] Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
| - | *[[Succinate | + | *[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]] |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 16:45, 3 November 2021
Crystal structure of the E. coli succinate:quinone oxidoreductase (SQR) SdhD His71Met mutant
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