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==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.==
<StructureSection load='5t25' size='340' side='right' caption='[[5t25]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
<StructureSection load='5t25' size='340' side='right'caption='[[5t25]], [[Resolution|resolution]] 1.99&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5t25]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T25 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T25 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5t25]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_IAI1 Escherichia coli IAI1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T25 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.991&#8491;</td></tr>
<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>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=74P:(E)-N~6~-(1-CARBOXY-3-OXOBUTYLIDENE)-L-LYSINE'>74P</scene>, <scene name='pdbligand=LYS:LYSINE'>LYS</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5t26|5t26]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5t25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t25 OCA], [https://pdbe.org/5t25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t25 RCSB], [https://www.ebi.ac.uk/pdbsum/5t25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t25 ProSAT]</span></td></tr>
<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=5t25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t25 OCA], [http://pdbe.org/5t25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t25 RCSB], [http://www.ebi.ac.uk/pdbsum/5t25 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t25 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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]  
[https://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]
 
==See Also==
*[[Dihydrodipicolinate synthase|Dihydrodipicolinate synthase]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: 4-hydroxy-tetrahydrodipicolinate synthase]]
[[Category: Escherichia coli IAI1]]
[[Category: Chooback, L]]
[[Category: Large Structures]]
[[Category: Fleming, C D]]
[[Category: Chooback L]]
[[Category: Karsten, W E]]
[[Category: Fleming CD]]
[[Category: Seabourn, P]]
[[Category: Karsten WE]]
[[Category: Thomas, L M]]
[[Category: Seabourn P]]
[[Category: Acetopyruvate modification]]
[[Category: Thomas LM]]
[[Category: Dihydrodipicolinate synthase]]
[[Category: Hydrolase]]
[[Category: Kinetic]]

Latest revision as of 15:53, 4 October 2023

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

5t25 is a 2 chain structure with sequence from Escherichia coli IAI1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.991Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DAPA_ECO8A Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA).[HAMAP-Rule:MF_00418]

See Also

5t25, resolution 1.99Å

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