4bqi
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==ARABIDOPSIS THALIANA cytosolic alpha-1,4-glucan phosphorylase (PHS2) in complex with maltotriose== | |
| + | <StructureSection load='4bqi' size='340' side='right'caption='[[4bqi]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4bqi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BQI 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]] 1.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PRD_900009:alpha-maltotriose'>PRD_900009</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=4bqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bqi OCA], [https://pdbe.org/4bqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bqi RCSB], [https://www.ebi.ac.uk/pdbsum/4bqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bqi ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PHS2_ARATH PHS2_ARATH] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties (By similarity). | ||
| - | + | ==See Also== | |
| - | + | *[[Polyl hydroxylase domain 3D structures|Polyl hydroxylase domain 3D structures]] | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Arabidopsis thaliana]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bornemann S]] | ||
| + | [[Category: Field RA]] | ||
| + | [[Category: Gunning AP]] | ||
| + | [[Category: Hetru AC]] | ||
| + | [[Category: Lawson DM]] | ||
| + | [[Category: Nepogodiev SA]] | ||
| + | [[Category: O'Neill EC]] | ||
| + | [[Category: Rashid AM]] | ||
| + | [[Category: Rejzek M]] | ||
| + | [[Category: Stevenson CEM]] | ||
Current revision
ARABIDOPSIS THALIANA cytosolic alpha-1,4-glucan phosphorylase (PHS2) in complex with maltotriose
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