1lqw: Difference between revisions

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[[Image:1lqw.png|left|200px]]


{{STRUCTURE_1lqw|  PDB=1lqw  |  SCENE=  }}
==Crystal Structure of S.aureus Peptide Deformylase==
 
<StructureSection load='1lqw' size='340' side='right'caption='[[1lqw]], [[Resolution|resolution]] 1.87&Aring;' scene=''>
===Crystal Structure of S.aureus Peptide Deformylase===
== Structural highlights ==
 
<table><tr><td colspan='2'>[[1lqw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LQW FirstGlance]. <br>
{{ABSTRACT_PUBMED_12126617}}
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
==About this Structure==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lqw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lqw OCA], [https://pdbe.org/1lqw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lqw RCSB], [https://www.ebi.ac.uk/pdbsum/1lqw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lqw ProSAT]</span></td></tr>
[[1lqw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LQW OCA].  
</table>
 
== Function ==
==Reference==
[https://www.uniprot.org/uniprot/DEF_STAAU DEF_STAAU] 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 (By similarity).[HAMAP-Rule:MF_00163]
<ref group="xtra">PMID:012126617</ref><references group="xtra"/>
== Evolutionary Conservation ==
[[Category: Peptide deformylase]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lq/1lqw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lqw ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Mikol, V.]]
[[Category: Mikol V]]
[[Category: Hydrolase]]
[[Category: Pdf]]
[[Category: Peptide deformylase]]

Latest revision as of 10:35, 14 February 2024

Crystal Structure of S.aureus Peptide DeformylaseCrystal Structure of S.aureus Peptide Deformylase

Structural highlights

1lqw is a 2 chain structure with sequence from Staphylococcus aureus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.87Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DEF_STAAU 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 (By similarity).[HAMAP-Rule:MF_00163]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1lqw, resolution 1.87Å

Drag the structure with the mouse to rotate

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OCA