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.
2p53
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2p53]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P53 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P53 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2p53]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P53 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2P53 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NNG:2-DEOXY-2-{[(S)-HYDROXY(METHYL)PHOSPHORYL]AMINO}-6-O-PHOSPHONO-ALPHA-D-GLUCOPYRANOSE'>NNG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NNG:2-DEOXY-2-{[(S)-HYDROXY(METHYL)PHOSPHORYL]AMINO}-6-O-PHOSPHONO-ALPHA-D-GLUCOPYRANOSE'>NNG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ymy|1ymy]], [[2p50|2p50]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ymy|1ymy]], [[2p50|2p50]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nagA, b0677, JW0663 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nagA, b0677, JW0663 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylglucosamine-6-phosphate_deacetylase N-acetylglucosamine-6-phosphate deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.25 3.5.1.25] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylglucosamine-6-phosphate_deacetylase N-acetylglucosamine-6-phosphate deacetylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.25 3.5.1.25] </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=2p53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p53 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2p53 RCSB], [http://www.ebi.ac.uk/pdbsum/2p53 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=2p53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p53 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2p53 RCSB], [http://www.ebi.ac.uk/pdbsum/2p53 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://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]] | ||
| Line 33: | Line 35: | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: N-acetylglucosamine-6-phosphate deacetylase]] | [[Category: N-acetylglucosamine-6-phosphate deacetylase]] | ||
| - | [[Category: Almo, S C | + | [[Category: Almo, S C]] |
| - | [[Category: Fedorov, A A | + | [[Category: Fedorov, A A]] |
| - | [[Category: Fedorov, E V | + | [[Category: Fedorov, E V]] |
| - | [[Category: Hall, R S | + | [[Category: Hall, R S]] |
| - | [[Category: Raushel, F M | + | [[Category: Raushel, F M]] |
[[Category: Aminohydrolase]] | [[Category: Aminohydrolase]] | ||
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: N-acetyl-d-glucosamine-6-phosphate deacetylase]] | [[Category: N-acetyl-d-glucosamine-6-phosphate deacetylase]] | ||
Revision as of 20:15, 24 December 2014
Crystal structure of N-acetyl-D-glucosamine-6-phosphate deacetylase D273N mutant complexed with N-acetyl phosphonamidate-d-glucosamine-6-phosphate
| |||||||||||
