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==The structure of E.coli peptide deformylase (PDF) in complex with peptidomimetic ligand BB2827==
==The structure of E.coli peptide deformylase (PDF) in complex with peptidomimetic ligand BB2827==
<StructureSection load='3k6l' size='340' side='right' caption='[[3k6l]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
<StructureSection load='3k6l' size='340' side='right'caption='[[3k6l]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3k6l]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3K6L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3K6L FirstGlance]. <br>
<table><tr><td colspan='2'>[[3k6l]] is a 3 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=3K6L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3K6L FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2BB:(2S,3R)-N~4~-[(1S)-1-(DIMETHYLCARBAMOYL)-2,2-DIMETHYLPROPYL]-N~1~,2-DIHYDROXY-3-(2-METHYLPROPYL)BUTANEDIAMIDE'>2BB</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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]] 2.15&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">def, fms, b3287, JW3248 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2BB:(2S,3R)-N~4~-[(1S)-1-(DIMETHYLCARBAMOYL)-2,2-DIMETHYLPROPYL]-N~1~,2-DIHYDROXY-3-(2-METHYLPROPYL)BUTANEDIAMIDE'>2BB</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] </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=3k6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k6l OCA], [https://pdbe.org/3k6l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3k6l RCSB], [https://www.ebi.ac.uk/pdbsum/3k6l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3k6l 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=3k6l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3k6l OCA], [http://pdbe.org/3k6l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3k6l RCSB], [http://www.ebi.ac.uk/pdbsum/3k6l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3k6l ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DEF_ECOLI DEF_ECOLI]] Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.[HAMAP-Rule:MF_00163]  
[https://www.uniprot.org/uniprot/DEF_ECOLI DEF_ECOLI] Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions.[HAMAP-Rule:MF_00163]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Ecoli]]
[[Category: Escherichia coli K-12]]
[[Category: Peptide deformylase]]
[[Category: Large Structures]]
[[Category: Barker, J]]
[[Category: Barker J]]
[[Category: Cheng, R K.Y]]
[[Category: Cheng RKY]]
[[Category: Crawley, L]]
[[Category: Crawley L]]
[[Category: Felicetti, B]]
[[Category: Felicetti B]]
[[Category: Whittaker, M]]
[[Category: Whittaker M]]
[[Category: Wood, M]]
[[Category: Wood M]]
[[Category: Hydrolase]]
[[Category: Ion binding]]
[[Category: Iron]]
[[Category: Metal-binding]]
[[Category: Protein biosynthesis]]
[[Category: Translation]]

Latest revision as of 08:10, 6 September 2023

The structure of E.coli peptide deformylase (PDF) in complex with peptidomimetic ligand BB2827

3k6l, resolution 2.15Å

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