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4uui
From Proteopedia
(Difference between revisions)
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| - | ''' | + | ==A case study for twinned data analysis: multiple crystal forms of the enzyme N-acetyl-neuraminic lyase== |
| - | + | <StructureSection load='4uui' size='340' side='right' caption='[[4uui]], [[Resolution|resolution]] 1.79Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4uui]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4UUI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UUI FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></td></tr> | |
| - | + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=KPI:(2S)-2-AMINO-6-[(1-HYDROXY-1-OXO-PROPAN-2-YLIDENE)AMINO]HEXANOIC+ACID'>KPI</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> | |
| - | [[ | + | <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=4uui FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4uui OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4uui RCSB], [http://www.ebi.ac.uk/pdbsum/4uui PDBsum]</span></td></tr> |
| - | [[ | + | </table> |
| - | [[Category: | + | == Function == |
| + | [[http://www.uniprot.org/uniprot/NANA_ECOLI NANA_ECOLI]] Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate.[HAMAP-Rule:MF_01237] | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: N-acetylneuraminate lyase]] | ||
[[Category: Campeotto, I]] | [[Category: Campeotto, I]] | ||
| + | [[Category: Pearson, A R]] | ||
| + | [[Category: Phillips, S E.V]] | ||
| + | [[Category: Aldolase]] | ||
| + | [[Category: Directed evolution]] | ||
| + | [[Category: Lyase]] | ||
| + | [[Category: N-acetylneuraminic acid lyase]] | ||
| + | [[Category: Protein engineering]] | ||
| + | [[Category: Substrate specificity]] | ||
| + | [[Category: Twinning]] | ||
Revision as of 14:47, 12 August 2015
A case study for twinned data analysis: multiple crystal forms of the enzyme N-acetyl-neuraminic lyase
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