This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2vgk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (15:19, 13 December 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='2vgk' size='340' side='right'caption='[[2vgk]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
<StructureSection load='2vgk' size='340' side='right'caption='[[2vgk]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[2vgk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomadura_sp. Actinomadura sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VGK FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[2vgk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Actinomadura_sp._R39 Actinomadura sp. R39]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VGK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VGK FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=REZ:(2R)-2-AMINO-7-{[(1R)-1-CARBOXYETHYL]AMINO}-7-OXOHEPTANOIC+ACID'>REZ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.25&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1w79|1w79]], [[1w8q|1w8q]], [[2vgj|2vgj]], [[1w8y|1w8y]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=REZ:(2R)-2-AMINO-7-{[(1R)-1-CARBOXYETHYL]AMINO}-7-OXOHEPTANOIC+ACID'>REZ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=2vgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vgk OCA], [https://pdbe.org/2vgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vgk RCSB], [https://www.ebi.ac.uk/pdbsum/2vgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vgk 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=2vgk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vgk OCA], [https://pdbe.org/2vgk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vgk RCSB], [https://www.ebi.ac.uk/pdbsum/2vgk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vgk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/DAC_ACTSP DAC_ACTSP]] Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors.
+
[https://www.uniprot.org/uniprot/DAC_ACTSP DAC_ACTSP] 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]]
Line 38: Line 37:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Actinomadura sp]]
+
[[Category: Actinomadura sp. R39]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Serine-type D-Ala-D-Ala carboxypeptidase]]
+
[[Category: Charlier P]]
-
[[Category: Charlier, P]]
+
[[Category: Herman R]]
-
[[Category: Herman, R]]
+
[[Category: Sauvage E]]
-
[[Category: Sauvage, E]]
+
[[Category: Kerff F]]
-
[[Category: Kerff, F]]
+
-
[[Category: Actinomadura]]
+
-
[[Category: Antibiotic resistance]]
+
-
[[Category: Carboxypeptidase]]
+
-
[[Category: Cell shape]]
+
-
[[Category: Cell wall biogenesis/degradation]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Penicillin-binding]]
+
-
[[Category: Peptidoglycan]]
+
-
[[Category: Peptidoglycan synthesis]]
+
-
[[Category: Protease]]
+
-
[[Category: Secreted]]
+
-
[[Category: Transpeptidase]]
+

Current revision

Crystal structure of Actinomadura R39 DD-peptidase complexed with a peptidoglycan-mimetic cephalosporin

PDB ID 2vgk

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2vgk"
Personal tools