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3tyk

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Current revision (12:47, 17 January 2024) (edit) (undo)
 
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<StructureSection load='3tyk' size='340' side='right'caption='[[3tyk]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='3tyk' size='340' side='right'caption='[[3tyk]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tyk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3ovc 3ovc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TYK FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tyk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3ovc 3ovc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TYK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TYK FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HY0:HYGROMYCIN+B+VARIANT'>HY0</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]] 1.95&#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=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSX:S-OXY+CYSTEINE'>CSX</scene>, <scene name='pdbligand=HY0:HYGROMYCIN+B+VARIANT'>HY0</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">APH(4), hph ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Hygromycin_B_4-O-kinase Hygromycin B 4-O-kinase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.163 2.7.1.163] </span></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=3tyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tyk OCA], [https://pdbe.org/3tyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tyk RCSB], [https://www.ebi.ac.uk/pdbsum/3tyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tyk 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=3tyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tyk OCA], [https://pdbe.org/3tyk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tyk RCSB], [https://www.ebi.ac.uk/pdbsum/3tyk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tyk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/KHYB_ECOLX KHYB_ECOLX]] The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation. Only phosphorylates hygromycin and closely related compounds such as demethyl analogs and destomycin.
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[https://www.uniprot.org/uniprot/KHYB_ECOLX KHYB_ECOLX] The aminoglycoside phosphotransferases achieve inactivation of their antibiotic substrates by phosphorylation. Only phosphorylates hygromycin and closely related compounds such as demethyl analogs and destomycin.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
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[[Category: Hygromycin B 4-O-kinase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Anderson, W F]]
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[[Category: Anderson WF]]
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[[Category: Chruszcz, M]]
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[[Category: Chruszcz M]]
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[[Category: Evdokmova, E]]
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[[Category: Evdokmova E]]
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[[Category: Fan, Y]]
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[[Category: Fan Y]]
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[[Category: Structural genomic]]
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[[Category: Minor W]]
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[[Category: Minor, W]]
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[[Category: Savchenko A]]
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[[Category: Savchenko, A]]
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[[Category: Shabalin IG]]
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[[Category: Shabalin, I G]]
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[[Category: Shakya T]]
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[[Category: Shakya, T]]
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[[Category: Stogios PJ]]
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[[Category: Stogios, P J]]
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[[Category: Wright GD]]
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[[Category: Wright, G D]]
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[[Category: Aminoglycoside binding]]
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[[Category: Aminoglycoside phosphotransferase]]
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[[Category: Antibiotic resistance]]
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[[Category: Cytoplasmic]]
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[[Category: Eukaryotic protein kinase-like fold]]
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[[Category: Mcsg]]
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[[Category: Phosphorylation]]
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[[Category: Phosphotransferase/kinase]]
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[[Category: PSI, Protein structure initiative]]
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[[Category: Transferase-antibiotic complex]]
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Current revision

Crystal structure of aminoglycoside phosphotransferase APH(4)-Ia

PDB ID 3tyk

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