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1adc
From Proteopedia
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| - | [[Image:1adc.png|left|200px]] | ||
| - | + | ==CRYSTALLOGRAPHIC STUDIES OF ISOSTERIC NAD ANALOGUES BOUND TO ALCOHOL DEHYDROGENASE: SPECIFICITY AND SUBSTRATE BINDING IN TWO TERNARY COMPLEXES== | |
| - | + | <StructureSection load='1adc' size='340' side='right'caption='[[1adc]], [[Resolution|resolution]] 2.70Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1adc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. The January 2001 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Alcohol Dehydrogenase'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2001_1 10.2210/rcsb_pdb/mom_2001_1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ADC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ADC 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]] 2.7Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=PAD:5-BETA-D-RIBOFURANOSYLPICOLINAMIDE+ADENINE-DINUCLEOTIDE'>PAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1adc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1adc OCA], [https://pdbe.org/1adc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1adc RCSB], [https://www.ebi.ac.uk/pdbsum/1adc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1adc ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/ADH1E_HORSE ADH1E_HORSE] | |
| - | + | == Evolutionary Conservation == | |
| - | < | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | + | Check<jmol> | |
| - | + | <jmolCheckbox> | |
| - | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ad/1adc_consurf.spt"</scriptWhenChecked> | |
| - | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |
| - | + | <text>to colour the structure by Evolutionary Conservation</text> | |
| - | == | + | </jmolCheckbox> |
| - | [[1adc]] is a 2 chain structure | + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1adc ConSurf]. |
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[Alcohol dehydrogenase|Alcohol dehydrogenase]] | + | *[[Alcohol dehydrogenase 3D structures|Alcohol dehydrogenase 3D structures]] |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
[[Category: Alcohol Dehydrogenase]] | [[Category: Alcohol Dehydrogenase]] | ||
| - | [[Category: Alcohol dehydrogenase]] | ||
[[Category: Equus caballus]] | [[Category: Equus caballus]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
| - | [[Category: Goldstein | + | [[Category: Goldstein BM]] |
| - | [[Category: Hallows | + | [[Category: Hallows WA]] |
| - | [[Category: Li | + | [[Category: Li H]] |
| - | [[Category: Pankiewicz | + | [[Category: Pankiewicz KW]] |
| - | [[Category: Punzi | + | [[Category: Punzi JS]] |
| - | [[Category: Watanabe | + | [[Category: Watanabe KA]] |
Current revision
CRYSTALLOGRAPHIC STUDIES OF ISOSTERIC NAD ANALOGUES BOUND TO ALCOHOL DEHYDROGENASE: SPECIFICITY AND SUBSTRATE BINDING IN TWO TERNARY COMPLEXES
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