9bbo: Difference between revisions
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==Proline utilization A complexed with the product L-glutamate in the aldehyde dehydrogenase active site== | |||
<StructureSection load='9bbo' size='340' side='right'caption='[[9bbo]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9bbo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Sinorhizobium_meliloti Sinorhizobium meliloti]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9BBO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9BBO FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | |||
[[Category: | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=GGL:GAMMA-L-GLUTAMIC+ACID'>GGL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=9bbo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9bbo OCA], [https://pdbe.org/9bbo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9bbo RCSB], [https://www.ebi.ac.uk/pdbsum/9bbo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9bbo ProSAT]</span></td></tr> | |||
</table> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Sinorhizobium meliloti]] | |||
[[Category: Tanner JJ]] | |||
Latest revision as of 10:28, 12 March 2025
Proline utilization A complexed with the product L-glutamate in the aldehyde dehydrogenase active site
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