2qn7: Difference between revisions

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<StructureSection load='2qn7' size='340' side='right'caption='[[2qn7]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
<StructureSection load='2qn7' size='340' side='right'caption='[[2qn7]], [[Resolution|resolution]] 1.83&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2qn7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QN7 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2QN7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2qn7]] 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=2QN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QN7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HBZ:N-{[(4-HYDROXYPHENYL)CARBONYL]CARBAMOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>HBZ</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HBZ:N-{[(4-HYDROXYPHENYL)CARBONYL]CARBAMOYL}-BETA-D-GLUCOPYRANOSYLAMINE'>HBZ</scene>, <scene name='pdbligand=IMP:INOSINIC+ACID'>IMP</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2qlm|2qlm]], [[2qln|2qln]], [[2qn3|2qn3]], [[2qn8|2qn8]], [[2qn9|2qn9]], [[2qnb|2qnb]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qlm|2qlm]], [[2qln|2qln]], [[2qn3|2qn3]], [[2qn8|2qn8]], [[2qn9|2qn9]], [[2qnb|2qnb]]</div></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphorylase Phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.1.1 2.4.1.1] </span></td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2qn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qn7 OCA], [http://pdbe.org/2qn7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qn7 RCSB], [http://www.ebi.ac.uk/pdbsum/2qn7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qn7 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=2qn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qn7 OCA], [https://pdbe.org/2qn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qn7 RCSB], [https://www.ebi.ac.uk/pdbsum/2qn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qn7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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.  
[[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]]

Revision as of 10:44, 16 March 2022

Glycogen Phosphorylase b in complex with N-4-hydroxybenzoyl-N'-4-beta-D-glucopyranosyl ureaGlycogen Phosphorylase b in complex with N-4-hydroxybenzoyl-N'-4-beta-D-glucopyranosyl urea

Structural highlights

2qn7 is a 1 chain structure with sequence from Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:Phosphorylase, with EC number 2.4.1.1
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2qn7, resolution 1.83Å

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