1es5: Difference between revisions

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<StructureSection load='1es5' size='340' side='right'caption='[[1es5]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
<StructureSection load='1es5' size='340' side='right'caption='[[1es5]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1es5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Strsk Strsk]. 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>
<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>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1skf|1skf]], [[1eqs|1eqs]], [[1es3|1es3]], [[1es4|1es4]], [[1esi|1esi]]</div></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]] 1.4&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Serine-type_D-Ala-D-Ala_carboxypeptidase Serine-type D-Ala-D-Ala carboxypeptidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.16.4 3.4.16.4] </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=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>
<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>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/DACX_STRSK DACX_STRSK]] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.  
[https://www.uniprot.org/uniprot/DACX_STRSK DACX_STRSK] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
[[Category: Streptomyces sp. K15]]
[[Category: Strsk]]
[[Category: Charlier P]]
[[Category: Charlier, P]]
[[Category: Fonze E]]
[[Category: Fonze, E]]
[[Category: Beta-lactamase]]
[[Category: Dd-transpeptidase]]
[[Category: Hydrolase]]
[[Category: Hydrolase carboxypeptidase]]
[[Category: Penicillin-binding]]
[[Category: Serine peptidase]]

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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