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4ock
From Proteopedia
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==N-acetylhexosamine 1-phosphate kinase in complex with GlcNAc and AMPPNP== | ==N-acetylhexosamine 1-phosphate kinase in complex with GlcNAc and AMPPNP== | ||
| - | <StructureSection load='4ock' size='340' side='right' caption='[[4ock]], [[Resolution|resolution]] 1.72Å' scene=''> | + | <StructureSection load='4ock' size='340' side='right'caption='[[4ock]], [[Resolution|resolution]] 1.72Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[4ock]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OCK OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[4ock]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum Bifidobacterium longum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OCK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OCK FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.72Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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=4ock FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ock OCA], [https://pdbe.org/4ock PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ock RCSB], [https://www.ebi.ac.uk/pdbsum/4ock PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ock ProSAT]</span></td></tr> | |
| - | + | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/NAHK_BIFL2 NAHK_BIFL2] Phosphorylates both N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) at similar rates. Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria. Also accepts GTP and ITP as phosphate donors. In vitro, can phosphorylate several GlcNAc and GalNAc derivatives.<ref>PMID:17720833</ref> <ref>PMID:19436918</ref> <ref>PMID:19683921</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 4ock" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Bifidobacterium longum]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Chang CY]] |
| - | [[Category: | + | [[Category: Li TL]] |
| - | [[Category: | + | [[Category: Liu YC]] |
| - | [[Category: | + | [[Category: Lyu SY]] |
| - | [[Category: | + | [[Category: Wang KC]] |
| - | [[Category: | + | [[Category: Wu CJ]] |
| - | + | ||
| - | + | ||
Current revision
N-acetylhexosamine 1-phosphate kinase in complex with GlcNAc and AMPPNP
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Categories: Bifidobacterium longum | Large Structures | Chang CY | Li TL | Liu YC | Lyu SY | Wang KC | Wu CJ
