This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
3cut
From Proteopedia
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3cut]] 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=3CUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CUT FirstGlance]. <br> | <table><tr><td colspan='2'>[[3cut]] 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=3CUT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CUT FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=179:N-[(NAPHTHALEN-2-YLAMINO)(OXO)ACETYL]-BETA-D-GLUCOPYRANOSYLAMINE'>179</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=179:N-[(NAPHTHALEN-2-YLAMINO)(OXO)ACETYL]-BETA-D-GLUCOPYRANOSYLAMINE'>179</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr> | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LLP:2-LYSINE(3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHANE)'>LLP</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cuu|3cuu]], [[3cuv|3cuv]], [[3cuw|3cuw]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3cuu|3cuu]], [[3cuv|3cuv]], [[3cuw|3cuw]]</td></tr> |
| - | <tr><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'>[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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cut OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cut RCSB], [http://www.ebi.ac.uk/pdbsum/3cut PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cut OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cut RCSB], [http://www.ebi.ac.uk/pdbsum/3cut PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == 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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 26: | Line 28: | ||
[[Category: Oryctolagus cuniculus]] | [[Category: Oryctolagus cuniculus]] | ||
[[Category: Phosphorylase]] | [[Category: Phosphorylase]] | ||
| - | [[Category: Chrysina, E D | + | [[Category: Chrysina, E D]] |
| - | [[Category: Kyritsi, C | + | [[Category: Kyritsi, C]] |
| - | [[Category: Leonidas, D D | + | [[Category: Leonidas, D D]] |
| - | [[Category: Oikonomakos, N G | + | [[Category: Oikonomakos, N G]] |
| - | [[Category: Zographos, S E | + | [[Category: Zographos, S E]] |
[[Category: Allosteric enzyme]] | [[Category: Allosteric enzyme]] | ||
[[Category: Carbohydrate metabolism]] | [[Category: Carbohydrate metabolism]] | ||
Revision as of 18:13, 25 December 2014
Crystal structure of glycogen phosphorylase b in complex with N-(-D-glucopyranosyl)-N'-(2-naphthyl)oxamide
| |||||||||||
Categories: Oryctolagus cuniculus | Phosphorylase | Chrysina, E D | Kyritsi, C | Leonidas, D D | Oikonomakos, N G | Zographos, S E | Allosteric enzyme | Carbohydrate metabolism | Catalytic site | Glycogen metabolism | Glycogen phosphorylase | Glycosyltransferase | Nucleotide-binding | Phosphoprotein | Pyridoxal phosphate | Rational inhibitor design | Transferase

