4eke
From Proteopedia
(Difference between revisions)
m (Protected "4eke" [edit=sysop:move=sysop]) |
|||
| (10 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of GPb in complex with DK11== | |
| + | <StructureSection load='4eke' size='340' side='right'caption='[[4eke]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4eke]] 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=4EKE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EKE 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]] 2.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=D1I:3-(BETA-D-GLUCOPYRANOSYL)-6-PENTYLFURO[2,3-D]PYRIMIDIN-2(3H)-ONE'>D1I</scene>, <scene name='pdbligand=LLP:(2S)-2-AMINO-6-[[3-HYDROXY-2-METHYL-5-(PHOSPHONOOXYMETHYL)PYRIDIN-4-YL]METHYLIDENEAMINO]HEXANOIC+ACID'>LLP</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=4eke FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eke OCA], [https://pdbe.org/4eke PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eke RCSB], [https://www.ebi.ac.uk/pdbsum/4eke PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eke ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [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. | ||
| - | + | ==See Also== | |
| - | + | *[[Glycogen phosphorylase 3D structures|Glycogen phosphorylase 3D structures]] | |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Oryctolagus cuniculus]] | ||
| + | [[Category: Kantsadi AL]] | ||
| + | [[Category: Leonidas DD]] | ||
| + | [[Category: Skamnaki VT]] | ||
Current revision
Crystal structure of GPb in complex with DK11
| |||||||||||
