4x0o: Difference between revisions
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<StructureSection load='4x0o' size='340' side='right'caption='[[4x0o]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='4x0o' size='340' side='right'caption='[[4x0o]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4x0o]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[4x0o]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae_O1_biovar_El_Tor_str._N16961 Vibrio cholerae O1 biovar El Tor str. N16961]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4X0O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4X0O FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene></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=4x0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x0o OCA], [https://pdbe.org/4x0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x0o RCSB], [https://www.ebi.ac.uk/pdbsum/4x0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x0o 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=4x0o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4x0o OCA], [https://pdbe.org/4x0o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4x0o RCSB], [https://www.ebi.ac.uk/pdbsum/4x0o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4x0o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/FABH2_VIBCH FABH2_VIBCH] 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.[HAMAP-Rule:MF_01815] | |||
==See Also== | ==See Also== | ||
| Line 19: | Line 16: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Vibrio cholerae O1 biovar El Tor str. N16961]] | ||
[[Category: Anderson | [[Category: Anderson WF]] | ||
[[Category: Chordia MD]] | |||
[[Category: Chordia | [[Category: Chruszcz M]] | ||
[[Category: Chruszcz | [[Category: Cooper DR]] | ||
[[Category: Cooper | [[Category: Hou J]] | ||
[[Category: Hou | [[Category: Minor W]] | ||
[[Category: Minor | [[Category: Zheng H]] | ||
[[Category: Zheng | [[Category: Zimmerman MD]] | ||
[[Category: Zimmerman | |||
Latest revision as of 10:39, 27 September 2023
Beta-ketoacyl-(acyl carrier protein) synthase III-2 (FabH2) from Vibrio cholerae soaked with Acetyl-CoABeta-ketoacyl-(acyl carrier protein) synthase III-2 (FabH2) from Vibrio cholerae soaked with Acetyl-CoA
Structural highlights
FunctionFABH2_VIBCH 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.[HAMAP-Rule:MF_01815] See Also |
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