4wzu

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:39, 27 September 2023) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
 +
==Crystal structure of beta-ketoacyl-(acyl carrier protein) synthase III-2 (FabH2) from Vibrio cholerae==
==Crystal structure of beta-ketoacyl-(acyl carrier protein) synthase III-2 (FabH2) from Vibrio cholerae==
-
<StructureSection load='4wzu' size='340' side='right' caption='[[4wzu]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
+
<StructureSection load='4wzu' size='340' side='right'caption='[[4wzu]], [[Resolution|resolution]] 1.88&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4wzu]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WZU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WZU FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4wzu]] is a 1 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=4WZU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WZU FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.88&#8491;</td></tr>
-
<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>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></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=4wzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wzu OCA], [http://pdbe.org/4wzu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wzu RCSB], [http://www.ebi.ac.uk/pdbsum/4wzu PDBsum]</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=4wzu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wzu OCA], [https://pdbe.org/4wzu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wzu RCSB], [https://www.ebi.ac.uk/pdbsum/4wzu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wzu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[http://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]
+
[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==
-
*[[Acyl carrier protein synthase|Acyl carrier protein synthase]]
+
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Anderson, W F]]
+
[[Category: Large Structures]]
-
[[Category: Structural genomic]]
+
[[Category: Vibrio cholerae O1 biovar El Tor str. N16961]]
-
[[Category: Chordia, M D]]
+
[[Category: Anderson WF]]
-
[[Category: Chruszcz, M]]
+
[[Category: Chordia MD]]
-
[[Category: Cooper, D R]]
+
[[Category: Chruszcz M]]
-
[[Category: Hou, J]]
+
[[Category: Cooper DR]]
-
[[Category: Minor, W]]
+
[[Category: Hou J]]
-
[[Category: Zheng, H]]
+
[[Category: Minor W]]
-
[[Category: Zimmerman, M D]]
+
[[Category: Zheng H]]
-
[[Category: Csgid]]
+
[[Category: Zimmerman MD]]
-
[[Category: Fabh]]
+
-
[[Category: Transferase]]
+

Current revision

Crystal structure of beta-ketoacyl-(acyl carrier protein) synthase III-2 (FabH2) from Vibrio cholerae

PDB ID 4wzu

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools