5kob: Difference between revisions

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==Crystal structure of a peptide deformylase from Burkholderia xenovorans==
==Crystal structure of a peptide deformylase from Burkholderia xenovorans==
<StructureSection load='5kob' size='340' side='right' caption='[[5kob]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
<StructureSection load='5kob' size='340' side='right'caption='[[5kob]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5kob]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Burkholderia_cepacia_lb400 Burkholderia cepacia lb400]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KOB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KOB FirstGlance]. <br>
<table><tr><td colspan='2'>[[5kob]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Paraburkholderia_xenovorans_LB400 Paraburkholderia xenovorans LB400]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KOB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KOB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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]] 1.6&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">def, Bxe_A1677 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=266265 Burkholderia cepacia LB400])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</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=5kob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kob OCA], [https://pdbe.org/5kob PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kob RCSB], [https://www.ebi.ac.uk/pdbsum/5kob PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kob 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=5kob FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kob OCA], [http://pdbe.org/5kob PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kob RCSB], [http://www.ebi.ac.uk/pdbsum/5kob PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kob ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/Q13XB1_BURXL Q13XB1_BURXL]] 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/Q13XB1_PARXL Q13XB1_PARXL] 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]
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Burkholderia cepacia lb400]]
[[Category: Large Structures]]
[[Category: Peptide deformylase]]
[[Category: Paraburkholderia xenovorans LB400]]
[[Category: SSGCID]]
[[Category: SSGCID]]
[[Category: Structural genomic]]
[[Category: Hydrolase]]
[[Category: Ssgcid]]

Latest revision as of 13:49, 27 September 2023

Crystal structure of a peptide deformylase from Burkholderia xenovoransCrystal structure of a peptide deformylase from Burkholderia xenovorans

Structural highlights

5kob is a 4 chain structure with sequence from Paraburkholderia xenovorans LB400. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q13XB1_PARXL 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]

5kob, resolution 1.60Å

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OCA