4uui: Difference between revisions

Line 1:

'''~~Unreleased structure~~'''

==A case study for twinned data analysis: multiple crystal forms of the enzyme N-acetyl-neuraminic lyase==

~~The entry~~ 4uui is ~~ON HOLD until Paper Publication~~

== 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 guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4UUI FirstGlance].

~~Authors~~: ~~Campeotto, I~~.~~, Phillips, S~~.E.V.~~, Pearson, A~~.R.

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</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">[[Non-Standard_Residue|NonStd Res:]]</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>

~~Description~~: ~~A case study for twinned data analysis~~: ~~multiple crystal forms of the enzyme~~ N-~~acetyl~~-~~neuraminic~~ lyase

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

[[~~Category~~: ~~Unreleased Structures~~]]

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[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]</td></tr>

[[~~Category~~: ~~Pearson, A~~.R]]

</table>

[[Category: ~~Phillips, S.E.V~~]]

== 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: 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]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==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]] 1.79&Aring;' scene=''>
-The entry 4uui is ON HOLD  until Paper Publication
+== 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>
-Authors: Campeotto, I., Phillips, S.E.V., Pearson, A.R.
+</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>
-Description: A case study for twinned data analysis: multiple crystal forms of the enzyme N-acetyl-neuraminic lyase
+<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: Unreleased Structures]]
+<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>
-[[Category: Pearson, A.R]]
+</table>
-[[Category: Phillips, S.E.V]]
+== 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: 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]]