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

Personal tools