5nn6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:10, 15 November 2023) (edit) (undo)
 
Line 1: Line 1:
==Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-hydroxyethyl-1-deoxynojirimycin==
==Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-hydroxyethyl-1-deoxynojirimycin==
-
<StructureSection load='5nn6' size='340' side='right' caption='[[5nn6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+
<StructureSection load='5nn6' size='340' side='right'caption='[[5nn6]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[5nn6]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NN6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NN6 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[5nn6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NN6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NN6 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MIG:(2R,3R,4R,5S)-1-(2-HYDROXYETHYL)-2-(HYDROXYMETHYL)PIPERIDINE-3,4,5-TRIOL'>MIG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</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&#8491;</td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MIG:(2R,3R,4R,5S)-1-(2-HYDROXYETHYL)-2-(HYDROXYMETHYL)PIPERIDINE-3,4,5-TRIOL'>MIG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5nn3|5nn3]], [[5nn4|5nn4]], [[5nn5|5nn5]]</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=5nn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nn6 OCA], [https://pdbe.org/5nn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nn6 RCSB], [https://www.ebi.ac.uk/pdbsum/5nn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nn6 ProSAT]</span></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GAA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-glucosidase Alpha-glucosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.20 3.2.1.20] </span></td></tr>
+
-
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nn6 OCA], [http://pdbe.org/5nn6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nn6 RCSB], [http://www.ebi.ac.uk/pdbsum/5nn6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nn6 ProSAT]</span></td></tr>
+
</table>
</table>
== Disease ==
== Disease ==
-
[[http://www.uniprot.org/uniprot/LYAG_HUMAN LYAG_HUMAN]] Glycogen storage disease due to acid maltase deficiency, infantile onset;Glycogen storage disease due to acid maltase deficiency, juvenile onset;Glycogen storage disease due to acid maltase deficiency, adult onset. The disease is caused by mutations affecting the gene represented in this entry.
+
[https://www.uniprot.org/uniprot/LYAG_HUMAN LYAG_HUMAN] Glycogen storage disease due to acid maltase deficiency, infantile onset;Glycogen storage disease due to acid maltase deficiency, juvenile onset;Glycogen storage disease due to acid maltase deficiency, adult onset. The disease is caused by mutations affecting the gene represented in this entry.
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/LYAG_HUMAN LYAG_HUMAN]] Essential for the degradation of glygogen to glucose in lysosomes.
+
[https://www.uniprot.org/uniprot/LYAG_HUMAN LYAG_HUMAN] Essential for the degradation of glygogen to glucose in lysosomes.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 24: Line 21:
</div>
</div>
<div class="pdbe-citations 5nn6" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5nn6" style="background-color:#fffaf0;"></div>
 +
 +
==See Also==
 +
*[[Alpha-glucosidase 3D structures|Alpha-glucosidase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Alpha-glucosidase]]
+
[[Category: Homo sapiens]]
-
[[Category: Human]]
+
[[Category: Large Structures]]
-
[[Category: Bourne, Y]]
+
[[Category: Bourne Y]]
-
[[Category: Cobucci-Ponzano, B]]
+
[[Category: Cobucci-Ponzano B]]
-
[[Category: Ferrara, M C]]
+
[[Category: Ferrara MC]]
-
[[Category: Germany, S]]
+
[[Category: Germany S]]
-
[[Category: Iacono, R]]
+
[[Category: Iacono R]]
-
[[Category: Moracci, M]]
+
[[Category: Moracci M]]
-
[[Category: Parenti, G]]
+
[[Category: Parenti G]]
-
[[Category: Roig-Zamboni, V]]
+
[[Category: Roig-Zamboni V]]
-
[[Category: Glycogen catabolism]]
+
-
[[Category: Glycoside hydrolase]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Lysosome]]
+
-
[[Category: Pompe disease]]
+

Current revision

Crystal structure of human lysosomal acid-alpha-glucosidase, GAA, in complex with N-hydroxyethyl-1-deoxynojirimycin

PDB ID 5nn6

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/5nn6"
Personal tools