2pd3: Difference between revisions

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<StructureSection load='2pd3' size='340' side='right'caption='[[2pd3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='2pd3' size='340' side='right'caption='[[2pd3]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2pd3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43504 Atcc 43504]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1jvf 1jvf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PD3 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2pd3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1jvf 1jvf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PD3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PD3 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</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]] 2.5&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2pd4|2pd4]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=TCL:TRICLOSAN'>TCL</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Enoyl-[acyl-carrier-protein]_reductase_(NADH) Enoyl-[acyl-carrier-protein] reductase (NADH)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.9 1.3.1.9] </span></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=2pd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pd3 OCA], [https://pdbe.org/2pd3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pd3 RCSB], [https://www.ebi.ac.uk/pdbsum/2pd3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pd3 ProSAT]</span></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=2pd3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pd3 OCA], [https://pdbe.org/2pd3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pd3 RCSB], [https://www.ebi.ac.uk/pdbsum/2pd3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pd3 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FABI_HELPY FABI_HELPY]] Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).  
[https://www.uniprot.org/uniprot/FABI_HELPY FABI_HELPY] Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 43504]]
[[Category: Helicobacter pylori]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lee, H H]]
[[Category: Lee HH]]
[[Category: Moon, J H]]
[[Category: Moon JH]]
[[Category: Suh, S W]]
[[Category: Suh SW]]
[[Category: Antibacterial target]]
[[Category: Enoyl-acp-reductase]]
[[Category: Fabi]]
[[Category: Helicobacter pylori]]
[[Category: Oxidoreductase]]
[[Category: Type ii fatty acid biosynthesis]]

Latest revision as of 12:00, 25 October 2023

Crystal Structure of the Helicobacter pylori Enoyl-Acyl Carrier Protein Reductase in Complex with Hydroxydiphenyl Ether Compounds, Triclosan and DiclosanCrystal Structure of the Helicobacter pylori Enoyl-Acyl Carrier Protein Reductase in Complex with Hydroxydiphenyl Ether Compounds, Triclosan and Diclosan

Structural highlights

2pd3 is a 4 chain structure with sequence from Helicobacter pylori. This structure supersedes the now removed PDB entry 1jvf. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FABI_HELPY Catalyzes the reduction of a carbon-carbon double bond in an enoyl moiety that is covalently linked to an acyl carrier protein (ACP). Involved in the elongation cycle of fatty acid which are used in the lipid metabolism (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2pd3, resolution 2.50Å

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