5lky: Difference between revisions
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==X-ray crystal structure of N-acetylneuraminic acid lyase in complex with pyruvate, with the phenylalanine at position 190 replaced with the non-canonical amino acid dihydroxypropylcysteine.== | |||
<StructureSection load='5lky' size='340' side='right' caption='[[5lky]], [[Resolution|resolution]] 1.70Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5lky]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LKY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LKY FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr> | |||
[[Category: | <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>, <scene name='pdbligand=P9S:DIHYDROXYPROPYLCYSTEINE'>P9S</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=5lky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lky OCA], [http://pdbe.org/5lky PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lky RCSB], [http://www.ebi.ac.uk/pdbsum/5lky PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lky ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/NANA_STAA8 NANA_STAA8]] Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate (By similarity). | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: N-acetylneuraminate lyase]] | |||
[[Category: Berry, A]] | |||
[[Category: Nelson, A S]] | |||
[[Category: Pearson, A R]] | |||
[[Category: Trinh, C H]] | |||
[[Category: Windle, C L]] | |||
[[Category: Aldolase]] | |||
[[Category: Lyase]] | |||
[[Category: Non-canonical amino acid]] | |||
[[Category: Tim barrel]] | |||
Revision as of 16:23, 22 March 2017
X-ray crystal structure of N-acetylneuraminic acid lyase in complex with pyruvate, with the phenylalanine at position 190 replaced with the non-canonical amino acid dihydroxypropylcysteine.
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