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.


3ljq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:36, 19 July 2023) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3ljq' size='340' side='right'caption='[[3ljq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
<StructureSection load='3ljq' size='340' side='right'caption='[[3ljq]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3ljq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_13253 Atcc 13253]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LJQ FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3ljq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LJQ FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.9&#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;'>[[9gaa|9gaa]], [[9gac|9gac]], [[9gaf|9gaf]], [[1p4v|1p4v]], [[1p4k|1p4k]]</div></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GA(1-295) ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=238 ATCC 13253])</td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.26 3.5.1.26] </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=3ljq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ljq OCA], [https://pdbe.org/3ljq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ljq RCSB], [https://www.ebi.ac.uk/pdbsum/3ljq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ljq 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=3ljq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ljq OCA], [https://pdbe.org/3ljq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ljq RCSB], [https://www.ebi.ac.uk/pdbsum/3ljq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ljq ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/ASPG_ELIMR ASPG_ELIMR]] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. Requires that the glycosylated asparagine moiety is not substituted on its N-(R1) and C- (R2) terminus.
+
[https://www.uniprot.org/uniprot/ASPG_ELIMR ASPG_ELIMR] Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins. Requires that the glycosylated asparagine moiety is not substituted on its N-(R1) and C- (R2) terminus.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 29: Line 27:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Atcc 13253]]
+
[[Category: Elizabethkingia meningoseptica]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Guo, H C]]
+
[[Category: Guo H-C]]
-
[[Category: Wang, Y]]
+
[[Category: Wang Y]]
-
[[Category: Active precursor]]
+
-
[[Category: Aspartylglucosylaminase]]
+
-
[[Category: Autoproteolysis]]
+
-
[[Category: Catalytic mechanism]]
+
-
[[Category: Constrained conformation]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: N-terminal nucleophile hydrolase]]
+
-
[[Category: Precursor structure]]
+
-
[[Category: Reversible inhibitor]]
+

Current revision

Crystal Structure of the Glycosylasparaginase T152C apo-precursor

PDB ID 3ljq

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/3ljq"
Personal tools