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4ryb

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<StructureSection load='4ryb' size='340' side='right'caption='[[4ryb]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
<StructureSection load='4ryb' size='340' side='right'caption='[[4ryb]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4ryb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Neimf Neimf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RYB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RYB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4ryb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Neisseria_meningitidis_FAM18 Neisseria meningitidis FAM18]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RYB FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qav|4qav]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ryb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryb OCA], [https://pdbe.org/4ryb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ryb RCSB], [https://www.ebi.ac.uk/pdbsum/4ryb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ryb ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272831 NEIMF])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-ketoacyl-[acyl-carrier-protein]_synthase_III Beta-ketoacyl-[acyl-carrier-protein] synthase III], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.180 2.3.1.180] </span></td></tr>
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<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=4ryb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ryb OCA], [http://pdbe.org/4ryb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ryb RCSB], [http://www.ebi.ac.uk/pdbsum/4ryb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ryb ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FABH_NEIMF FABH_NEIMF]] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
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[https://www.uniprot.org/uniprot/FABH_NEIMF FABH_NEIMF] Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids.
==See Also==
==See Also==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Neimf]]
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[[Category: Neisseria meningitidis FAM18]]
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[[Category: Forwood, J K]]
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[[Category: Forwood JK]]
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[[Category: Nanson, J D]]
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[[Category: Nanson JD]]
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[[Category: Condensing enzyme]]
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[[Category: Fabh]]
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[[Category: Kasiii]]
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[[Category: Thiolase fold]]
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[[Category: Transferase]]
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Current revision

Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Neisseria meningitidis

PDB ID 4ryb

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