5t26: Difference between revisions
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==Kinetic, Spectral and Structural Characterization of the Slow Binding Inhibitor Acetopyruvate with Dihydrodipicolinate Synthase from Escherichia coli.== | |||
<StructureSection load='5t26' size='340' side='right' caption='[[5t26]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5t26]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T26 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> | |||
[[Category: | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=74P:(E)-N~6~-(1-CARBOXY-3-OXOBUTYLIDENE)-L-LYSINE'>74P</scene></td></tr> | ||
[[Category: | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5t25|5t25]]</td></tr> | ||
[[Category: | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/4-hydroxy-tetrahydrodipicolinate_synthase 4-hydroxy-tetrahydrodipicolinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.3.3.7 4.3.3.7] </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=5t26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t26 OCA], [http://pdbe.org/5t26 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t26 RCSB], [http://www.ebi.ac.uk/pdbsum/5t26 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t26 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/DAPA_ECO8A DAPA_ECO8A]] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418] | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]] | |||
[[Category: Chooback, L]] | |||
[[Category: Fleming, C D]] | |||
[[Category: Karsten, W E]] | |||
[[Category: Seabourn, P]] | [[Category: Seabourn, P]] | ||
[[Category: | [[Category: Thomas, L M]] | ||
[[Category: | [[Category: Acetopyruvate modification]] | ||
[[Category: Dihydrodipicolinate synthase]] | |||
[[Category: Kinetic]] | |||
[[Category: Lyase]] |
Revision as of 00:45, 6 October 2016
Kinetic, Spectral and Structural Characterization of the Slow Binding Inhibitor Acetopyruvate with Dihydrodipicolinate Synthase from Escherichia coli.Kinetic, Spectral and Structural Characterization of the Slow Binding Inhibitor Acetopyruvate with Dihydrodipicolinate Synthase from Escherichia coli.
Structural highlights
Function[DAPA_ECO8A] Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418] |
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