5hm3: Difference between revisions
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==2.25 Angstrom Resolution Crystal Structure of Long-chain-fatty-acid-AMP Ligase FadD32 from Mycobacterium tuberculosis in complex with Inhibitor 5'-O-[(11-phenoxyundecanoyl)sulfamoyl]adenosine== | |||
<StructureSection load='5hm3' size='340' side='right' caption='[[5hm3]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5hm3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HM3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HM3 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=649:5-O-[(11-PHENOXYUNDECANOYL)SULFAMOYL]ADENOSINE'>649</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | |||
[[Category: | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=5hm3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hm3 OCA], [http://pdbe.org/5hm3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hm3 RCSB], [http://www.ebi.ac.uk/pdbsum/5hm3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hm3 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/FAA32_MYCTU FAA32_MYCTU]] Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the multifunctional polyketide synthase (PKS) for further chain extension.<ref>PMID:15042094</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aldrich, C C]] | |||
[[Category: Anderson, W A]] | |||
[[Category: Structural genomic]] | |||
[[Category: Flores, K J]] | |||
[[Category: Grimes, K D]] | |||
[[Category: Kuhn, M L]] | |||
[[Category: Minasov, G]] | |||
[[Category: Shuvalova, L]] | |||
[[Category: Warwrzak, Z]] | |||
[[Category: Wilson, D J]] | |||
[[Category: Csgid]] | |||
[[Category: Fadd32]] | |||
[[Category: Ligase-ligase inhibitor complex]] | |||
[[Category: Long-chain-fatty-acid--amp ligase]] | |||
Revision as of 04:15, 4 August 2016
2.25 Angstrom Resolution Crystal Structure of Long-chain-fatty-acid-AMP Ligase FadD32 from Mycobacterium tuberculosis in complex with Inhibitor 5'-O-[(11-phenoxyundecanoyl)sulfamoyl]adenosine
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