1h5u

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Current revision (12:17, 13 December 2023) (edit) (undo)
 
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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1h5u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H5U FirstGlance]. <br>
<table><tr><td colspan='2'>[[1h5u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H5U 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=CHI:5-CHLORO-1H-INDOLE-2-CARBOXYLIC+ACID+[1-(4-FLUOROBENZYL)-2-(4-HYDROXYPIPERIDIN-1YL)-2-OXOETHYL]AMIDE'>CHI</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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]] 1.76&#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;'>[[1a8i|1a8i]], [[1abb|1abb]], [[1axr|1axr]], [[1b4d|1b4d]], [[1bx3|1bx3]], [[1c50|1c50]], [[1c8k|1c8k]], [[1c8l|1c8l]], [[1e1y|1e1y]], [[1fs4|1fs4]], [[1ftq|1ftq]], [[1ftw|1ftw]], [[1fty|1fty]], [[1fu4|1fu4]], [[1fu7|1fu7]], [[1fu8|1fu8]], [[1gfz|1gfz]], [[1gg8|1gg8]], [[1ggn|1ggn]], [[1gpa|1gpa]], [[1gpb|1gpb]], [[1gpy|1gpy]], [[1hlf|1hlf]], [[1noi|1noi]], [[1noj|1noj]], [[1nok|1nok]], [[1pyg|1pyg]], [[2amv|2amv]], [[2gpa|2gpa]], [[2gpb|2gpb]], [[2gpn|2gpn]], [[2pri|2pri]], [[2prj|2prj]], [[2skc|2skc]], [[2skd|2skd]], [[2ske|2ske]], [[3amv|3amv]], [[3gpb|3gpb]], [[4gpb|4gpb]], [[5gpb|5gpb]], [[6gpb|6gpb]], [[7gpb|7gpb]], [[8gpb|8gpb]], [[9gpb|9gpb]]</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=CHI:5-CHLORO-1H-INDOLE-2-CARBOXYLIC+ACID+[1-(4-FLUOROBENZYL)-2-(4-HYDROXYPIPERIDIN-1YL)-2-OXOETHYL]AMIDE'>CHI</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</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=1h5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5u OCA], [https://pdbe.org/1h5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h5u RCSB], [https://www.ebi.ac.uk/pdbsum/1h5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h5u 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=1h5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h5u OCA], [https://pdbe.org/1h5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h5u RCSB], [https://www.ebi.ac.uk/pdbsum/1h5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h5u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT]] 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.
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[https://www.uniprot.org/uniprot/PYGM_RABIT PYGM_RABIT] 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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Oryctolagus cuniculus]]
[[Category: Oryctolagus cuniculus]]
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[[Category: Phosphorylase]]
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[[Category: Archontis G]]
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[[Category: Archontis, G]]
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[[Category: Oikonomakos NG]]
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[[Category: Oikonomakos, N G]]
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[[Category: Skamnaki VT]]
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[[Category: Skamnaki, V T]]
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[[Category: Zographos SE]]
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[[Category: Zographos, S E]]
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[[Category: Central cavity]]
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[[Category: Drug binding site]]
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[[Category: Glycogen metabolism]]
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[[Category: Glycogen phosphorylase b]]
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[[Category: Inhibition]]
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[[Category: Transferase]]
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Current revision

THE 1.76 A RESOLUTION CRYSTAL STRUCTURE OF GLYCOGEN PHOSPHORYLASE B COMPLEXED WITH GLUCOSE AND CP320626, A POTENTIAL ANTIDIABETIC DRUG

PDB ID 1h5u

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