1es5: Difference between revisions

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[[Image:1es5.jpg|left|200px]]


{{Structure
==S216A MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE==
|PDB= 1es5 |SIZE=350|CAPTION= <scene name='initialview01'>1es5</scene>, resolution 1.40&Aring;
<StructureSection load='1es5' size='340' side='right'caption='[[1es5]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1es5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._K15 Streptomyces sp. K15]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ES5 FirstGlance]. <br>
|ACTIVITY= [http://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4]  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1es5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1es5 OCA], [https://pdbe.org/1es5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1es5 RCSB], [https://www.ebi.ac.uk/pdbsum/1es5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1es5 ProSAT]</span></td></tr>
}}
</table>
== Function ==
[https://www.uniprot.org/uniprot/DACX_STRSK DACX_STRSK] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
== Evolutionary Conservation ==
[[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/es/1es5_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=1es5 ConSurf].
<div style="clear:both"></div>


'''S216A MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE'''
==See Also==
 
*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
 
*[[Penicillin-binding protein 3D structures|Penicillin-binding protein 3D structures]]
==About this Structure==
__TOC__
1ES5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ES5 OCA].
</StructureSection>
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Streptomyces sp. K15]]
[[Category: Streptomyces sp.]]
[[Category: Charlier P]]
[[Category: Charlier, P.]]
[[Category: Fonze E]]
[[Category: Fonze, E.]]
[[Category: beta-lactamase]]
[[Category: dd-transpeptidase]]
[[Category: hydrolase carboxypeptidase]]
[[Category: penicillin-binding]]
[[Category: serine peptidase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:59:38 2008''

Latest revision as of 10:06, 7 February 2024

S216A MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASES216A MUTANT OF STREPTOMYCES K15 DD-TRANSPEPTIDASE

Structural highlights

1es5 is a 1 chain structure with sequence from Streptomyces sp. K15. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.4Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DACX_STRSK Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.

Evolutionary Conservation

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

See Also

1es5, resolution 1.40Å

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