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1bsz

From Proteopedia

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Current revision (05:42, 9 August 2023) (edit) (undo)
 
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<StructureSection load='1bsz' size='340' side='right'caption='[[1bsz]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='1bsz' size='340' side='right'caption='[[1bsz]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1bsz]] 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=1BSZ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1BSZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1bsz]] 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=1BSZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BSZ 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=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bs5|1bs5]], [[1bs6|1bs6]], [[1bs7|1bs7]], [[1bs8|1bs8]]</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=2PE:NONAETHYLENE+GLYCOL'>2PE</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DEF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=1bsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsz OCA], [https://pdbe.org/1bsz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bsz RCSB], [https://www.ebi.ac.uk/pdbsum/1bsz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bsz ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Formylmethionine_deformylase Formylmethionine deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.31 3.5.1.31] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1bsz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsz OCA], [http://pdbe.org/1bsz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bsz RCSB], [http://www.ebi.ac.uk/pdbsum/1bsz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bsz ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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]
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[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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</div>
</div>
<div class="pdbe-citations 1bsz" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1bsz" style="background-color:#fffaf0;"></div>
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==See Also==
 
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*[[Unusual sequence numbering|Unusual sequence numbering]]
 
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Ecoli]]
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[[Category: Escherichia coli K-12]]
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[[Category: Formylmethionine deformylase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Becker, A]]
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[[Category: Becker A]]
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[[Category: Groche, D]]
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[[Category: Groche D]]
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[[Category: Kabsch, W]]
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[[Category: Kabsch W]]
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[[Category: Schlichting, I]]
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[[Category: Schlichting I]]
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[[Category: Schultz, S]]
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[[Category: Schultz S]]
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[[Category: Wagner, A F.V]]
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[[Category: Wagner AFV]]
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[[Category: Hydrolase]]
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[[Category: Iron metalloprotease]]
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[[Category: Protein synthesis]]
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Current revision

PEPTIDE DEFORMYLASE AS FE2+ CONTAINING FORM (NATIVE) IN COMPLEX WITH INHIBITOR POLYETHYLENE GLYCOL

PDB ID 1bsz

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