4bqi

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Current revision (11:56, 20 December 2023) (edit) (undo)
 
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<StructureSection load='4bqi' size='340' side='right'caption='[[4bqi]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='4bqi' size='340' side='right'caption='[[4bqi]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4bqi]] is a 2 chain structure. 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>
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<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>
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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=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></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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4bqe|4bqe]], [[4bqf|4bqf]]</div></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=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>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </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=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>
<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>
</table>
== Function ==
== Function ==
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[[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).
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[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==
==See Also==
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*[[Prolyl hydroxylase domain|Prolyl hydroxylase domain]]
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*[[Polyl hydroxylase domain 3D structures|Polyl hydroxylase domain 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Phosphorylase]]
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[[Category: Bornemann S]]
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[[Category: Bornemann, S]]
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[[Category: Field RA]]
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[[Category: Field, R A]]
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[[Category: Gunning AP]]
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[[Category: Gunning, A P]]
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[[Category: Hetru AC]]
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[[Category: Hetru, A C]]
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[[Category: Lawson DM]]
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[[Category: Lawson, D M]]
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[[Category: Nepogodiev SA]]
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[[Category: Neill, E C.O]]
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[[Category: O'Neill EC]]
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[[Category: Nepogodiev, S A]]
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[[Category: Rashid AM]]
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[[Category: Rashid, A M]]
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[[Category: Rejzek M]]
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[[Category: Rejzek, M]]
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[[Category: Stevenson CEM]]
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[[Category: Stevenson, C E.M]]
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[[Category: Carbohydrate metabolism]]
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[[Category: Self-assembly on surface]]
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[[Category: Transferase]]
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Current revision

ARABIDOPSIS THALIANA cytosolic alpha-1,4-glucan phosphorylase (PHS2) in complex with maltotriose

PDB ID 4bqi

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OCA

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