5f9s: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry 5f9s is ON HOLD until Paper Publication~~

==Crystal structure of human Alanine:Glyoxylate Aminotransferase major allele (AGT-Ma) at 1.7 Angstrom; internal aldimine with PLP in the active site==

~~Authors: Giardina, G., Cutruzzola, F., Borri Voltattorni, C., Cellini, B., Montioli, R.~~

== Structural highlights ==

<table><tr><td colspan='2'>[[5f9s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F9S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F9S FirstGlance]. <br>

~~Description:~~ Crystal structure of human Alanine:Glyoxylate Aminotransferase major allele (AGT-Ma) at 1.7 Angstrom; internal aldimine with PLP in the active site

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>

[[Category: ~~Unreleased Structures~~]]

<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=5f9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f9s OCA], [http://pdbe.org/5f9s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f9s RCSB], [http://www.ebi.ac.uk/pdbsum/5f9s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f9s ProSAT]</span></td></tr>

[[Category: ~~Borri Voltattorni~~, C]]

</table>

== Disease ==

[[http://www.uniprot.org/uniprot/SPYA_HUMAN SPYA_HUMAN]] Defects in AGXT are the cause of hyperoxaluria primary type 1 (HP1) [MIM:[http://omim.org/entry/259900 259900]]; also known as primary hyperoxaluria type I (PH1) and oxalosis I. HP1 is a rare autosomal recessive inborn error of glyoxylate metabolism characterized by increased excretion of oxalate and glycolate, and the progressive accumulation of insoluble calcium oxalate in the kidney and urinary tract.<ref>PMID:1703535</ref> <ref>PMID:2039493</ref> <ref>PMID:1349575</ref> <ref>PMID:1301173</ref> <ref>PMID:8101040</ref> <ref>PMID:9192270</ref> <ref>PMID:9604803</ref> <ref>PMID:10394939</ref> <ref>PMID:10453743</ref> <ref>PMID:10541294</ref> <ref>PMID:10862087</ref> <ref>PMID:10960483</ref> <ref>PMID:12559847</ref> <ref>PMID:12777626</ref> <ref>PMID:15253729</ref> <ref>PMID:15849466</ref> <ref>PMID:15961946</ref> <ref>PMID:15963748</ref>

== References ==

__TOC__

</StructureSection>

[[Category: Cellini, B]]

[[Category: Cutruzzola, F]]

[[Category: Giardina, G]]

[[Category: Montioli, R]]

[[Category: ~~Cutruzzola~~, F]]

[[Category: Voltattorni, C Borri]]

[[Category: ~~Cellini, B~~]]

[[Category: Aminotransferase]]

[[Category: Detoxification]]

[[Category: Liver]]

[[Category: Transferase]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5f9s is ON HOLD  until Paper Publication
+==Crystal structure of human Alanine:Glyoxylate Aminotransferase major allele (AGT-Ma) at 1.7 Angstrom; internal aldimine with PLP in the active site==
+<StructureSection load='5f9s' size='340' side='right' caption='[[5f9s]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
-Authors: Giardina, G., Cutruzzola, F., Borri Voltattorni, C., Cellini, B., Montioli, R.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5f9s]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F9S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F9S FirstGlance]. <br>
-Description: Crystal structure of human Alanine:Glyoxylate Aminotransferase major allele (AGT-Ma) at 1.7 Angstrom; internal aldimine with PLP in the active site
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-[[Category: Unreleased Structures]]
+<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=5f9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f9s OCA], [http://pdbe.org/5f9s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f9s RCSB], [http://www.ebi.ac.uk/pdbsum/5f9s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f9s ProSAT]</span></td></tr>
-[[Category: Borri Voltattorni, C]]
+</table>
+== Disease ==
+[[http://www.uniprot.org/uniprot/SPYA_HUMAN SPYA_HUMAN]] Defects in AGXT are the cause of hyperoxaluria primary type 1 (HP1) [MIM:[http://omim.org/entry/259900 259900]]; also known as primary hyperoxaluria type I (PH1) and oxalosis I. HP1 is a rare autosomal recessive inborn error of glyoxylate metabolism characterized by increased excretion of oxalate and glycolate, and the progressive accumulation of insoluble calcium oxalate in the kidney and urinary tract.<ref>PMID:1703535</ref> <ref>PMID:2039493</ref> <ref>PMID:1349575</ref> <ref>PMID:1301173</ref> <ref>PMID:8101040</ref> <ref>PMID:9192270</ref> <ref>PMID:9604803</ref> <ref>PMID:10394939</ref> <ref>PMID:10453743</ref> <ref>PMID:10541294</ref> <ref>PMID:10862087</ref> <ref>PMID:10960483</ref> <ref>PMID:12559847</ref> <ref>PMID:12777626</ref> <ref>PMID:15253729</ref> <ref>PMID:15849466</ref> <ref>PMID:15961946</ref> <ref>PMID:15963748</ref>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Cellini, B]]
+[[Category: Cutruzzola, F]]
 [[Category: Giardina, G]]
 [[Category: Montioli, R]]
-[[Category: Cutruzzola, F]]
+[[Category: Voltattorni, C Borri]]
-[[Category: Cellini, B]]
+[[Category: Aminotransferase]]
+[[Category: Detoxification]]
+[[Category: Liver]]
+[[Category: Transferase]]