6arh
From Proteopedia
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			| m  (Protected "6arh" [edit=sysop:move=sysop]) | |||
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Human NAL at a resolution of 1.6 Angstrom== | |
| - | + | <StructureSection load='6arh' size='340' side='right' caption='[[6arh]], [[Resolution|resolution]] 1.60Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[6arh]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ARH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ARH FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | |
| - | [[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/N-acetylneuraminate_lyase N-acetylneuraminate lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.3 4.1.3.3] </span></td></tr> | 
| - | [[Category:  | + | <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=6arh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6arh OCA], [http://pdbe.org/6arh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6arh RCSB], [http://www.ebi.ac.uk/pdbsum/6arh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6arh ProSAT]</span></td></tr> | 
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/NPL_HUMAN NPL_HUMAN]] Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. It prevents sialic acids from being recycled and returning to the cell surface. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. Although human is not able to catalyze formation of Neu5Gc due to the inactive CMAHP enzyme, Neu5Gc is present in food and must be degraded (By similarity).  | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: N-acetylneuraminate lyase]] | ||
| [[Category: Bundela, R]] | [[Category: Bundela, R]] | ||
| - | [[Category: Pearce, F | + | [[Category: Keown, J R]] | 
| + | [[Category: Pearce, F G]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: Sialic acid]] | ||
| + | [[Category: Sugar metabolism]] | ||
| + | [[Category: Tetramer]] | ||
Revision as of 06:03, 22 August 2018
Crystal structure of Human NAL at a resolution of 1.6 Angstrom
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