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2p50
From Proteopedia
(Difference between revisions)
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==Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn== | ==Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn== | ||
| - | <StructureSection load='2p50' size='340' side='right' caption='[[2p50]], [[Resolution|resolution]] 2.20Å' scene=''> | + | <StructureSection load='2p50' size='340' side='right'caption='[[2p50]], [[Resolution|resolution]] 2.20Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2p50]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2p50]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P50 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ymy|1ymy]], [[2p53|2p53]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ymy|1ymy]], [[2p53|2p53]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nagA, b0677, JW0663 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nagA, b0677, JW0663 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N-acetylglucosamine-6-phosphate_deacetylase N-acetylglucosamine-6-phosphate deacetylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.25 3.5.1.25] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p50 OCA], [https://pdbe.org/2p50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p50 RCSB], [https://www.ebi.ac.uk/pdbsum/2p50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p50 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/NAGA_ECOLI NAGA_ECOLI]] Catalyzes the deacetylation of N-acetyl-D-glucosamine-6-phosphate. In vitro, can also hydrolyze substrate analogs such as N-thioacetyl-D-glucosamine-6-phosphate, N-trifluoroacetyl-D-glucosamine-6-phosphate, N-acetyl-D-glucosamine-6-sulfate, N-acetyl-D-galactosamine-6-phosphate, and N-formyl-D-glucosamine-6-phosphate.<ref>PMID:17567047</ref> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Ecoli]] | [[Category: Ecoli]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: N-acetylglucosamine-6-phosphate deacetylase]] | [[Category: N-acetylglucosamine-6-phosphate deacetylase]] | ||
[[Category: Almo, S C]] | [[Category: Almo, S C]] | ||
Revision as of 15:16, 17 June 2021
Crystal structure of N-acetyl-D-Glucosamine-6-Phosphate deacetylase liganded with Zn
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