5bns

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (12:17, 6 March 2024) (edit) (undo)
 
(3 intermediate revisions not shown.)
Line 1: Line 1:
==E. coli Fabh with small molecule inhibitor 2==
==E. coli Fabh with small molecule inhibitor 2==
-
<StructureSection load='5bns' size='340' side='right' caption='[[5bns]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+
<StructureSection load='5bns' size='340' side='right'caption='[[5bns]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5bns]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BNS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BNS FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5bns]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BNS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BNS FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4VM:1-{5-[2-FLUORO-5-(HYDROXYMETHYL)PHENYL]PYRIDIN-2-YL}-N-(QUINOLIN-6-YLMETHYL)PIPERIDINE-4-CARBOXAMIDE'>4VM</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]] 2.2&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5bnm|5bnm]], [[5bnr|5bnr]], [[5bqs|5bqs]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4VM:1-{5-[2-FLUORO-5-(HYDROXYMETHYL)PHENYL]PYRIDIN-2-YL}-N-(QUINOLIN-6-YLMETHYL)PIPERIDINE-4-CARBOXAMIDE'>4VM</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5bns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bns OCA], [https://pdbe.org/5bns PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5bns RCSB], [https://www.ebi.ac.uk/pdbsum/5bns PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5bns ProSAT]</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=5bns FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5bns OCA], [http://pdbe.org/5bns PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5bns RCSB], [http://www.ebi.ac.uk/pdbsum/5bns PDBsum]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/FABH_ECOLI FABH_ECOLI]] 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. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain.[HAMAP-Rule:MF_01815]
+
[https://www.uniprot.org/uniprot/FABH_ECOLI FABH_ECOLI] 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. Has some substrate specificity for acetyl-CoA. Its substrate specificity determines the biosynthesis of straight-chain of fatty acids instead of branched-chain.[HAMAP-Rule:MF_01815]
 +
 
 +
==See Also==
 +
*[[Acyl carrier protein synthase 3D structures|Acyl carrier protein synthase 3D structures]]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Kazmirski, S L]]
+
[[Category: Escherichia coli K-12]]
-
[[Category: McKinney, D C]]
+
[[Category: Large Structures]]
-
[[Category: Anti-bacterial]]
+
[[Category: Kazmirski SL]]
-
[[Category: Fabh]]
+
[[Category: McKinney DC]]
-
[[Category: Fatty acid synthesis]]
+
-
[[Category: Transferase-transferase inhibitor complex]]
+

Current revision

E. coli Fabh with small molecule inhibitor 2

PDB ID 5bns

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools