1qh3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1qh3.jpg|left|200px]]<br /><applet load="1qh3" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1qh3.jpg|left|200px]]
-
caption="1qh3, resolution 1.9&Aring;" />
+
 
-
'''HUMAN GLYOXALASE II WITH CACODYLATE AND ACETATE IONS PRESENT IN THE ACTIVE SITE'''<br />
+
{{Structure
 +
|PDB= 1qh3 |SIZE=350|CAPTION= <scene name='initialview01'>1qh3</scene>, resolution 1.9&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Hydroxyacylglutathione_hydrolase Hydroxyacylglutathione hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.6 3.1.2.6]
 +
|GENE=
 +
}}
 +
 
 +
'''HUMAN GLYOXALASE II WITH CACODYLATE AND ACETATE IONS PRESENT IN THE ACTIVE SITE'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==About this Structure==
==About this Structure==
-
1QH3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CAC:'>CAC</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Hydroxyacylglutathione_hydrolase Hydroxyacylglutathione hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.2.6 3.1.2.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QH3 OCA].
+
1QH3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QH3 OCA].
==Reference==
==Reference==
-
Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue., Cameron AD, Ridderstrom M, Olin B, Mannervik B, Structure. 1999 Sep 15;7(9):1067-78. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10508780 10508780]
+
Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue., Cameron AD, Ridderstrom M, Olin B, Mannervik B, Structure. 1999 Sep 15;7(9):1067-78. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10508780 10508780]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Hydroxyacylglutathione hydrolase]]
[[Category: Hydroxyacylglutathione hydrolase]]
Line 28: Line 37:
[[Category: metallo-hydrolase]]
[[Category: metallo-hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:39:29 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:37:20 2008''

Revision as of 11:37, 20 March 2008

Image:1qh3.jpg


PDB ID 1qh3

Drag the structure with the mouse to rotate
, resolution 1.9Å
Ligands: , , , and
Activity: Hydroxyacylglutathione hydrolase, with EC number 3.1.2.6
Coordinates: save as pdb, mmCIF, xml



HUMAN GLYOXALASE II WITH CACODYLATE AND ACETATE IONS PRESENT IN THE ACTIVE SITE


Contents

Overview

BACKGROUND: Glyoxalase II, the second of two enzymes in the glyoxalase system, is a thiolesterase that catalyses the hydrolysis of S-D-lactoylglutathione to form glutathione and D-lactic acid. RESULTS: The structure of human glyoxalase II was solved initially by single isomorphous replacement with anomalous scattering and refined at a resolution of 1.9 A. The enzyme consists of two domains. The first domain folds into a four-layered beta sandwich, similar to that seen in the metallo-beta-lactamases. The second domain is predominantly alpha-helical. The active site contains a binuclear zinc-binding site and a substrate-binding site extending over the domain interface. The model contains acetate and cacodylate in the active site. A second complex was derived from crystals soaked in a solution containing the slow substrate, S-(N-hydroxy-N-bromophenylcarbamoyl)glutathione. This complex was refined at a resolution of 1.45 A. It contains the added ligand in one molecule of the asymmetric unit and glutathione in the other. CONCLUSIONS: The arrangement of ligands around the zinc ions includes a water molecule, presumably in the form of a hydroxide ion, coordinated to both metal ions. This hydroxide ion is situated 2.9 A from the carbonyl carbon of the substrate in such a position that it could act as the nucleophile during catalysis. The reaction mechanism may also have implications for the action of metallo-beta-lactamases.

Disease

Known diseases associated with this structure: Glyoxalase II deficiency OMIM:[138760]

About this Structure

1QH3 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue., Cameron AD, Ridderstrom M, Olin B, Mannervik B, Structure. 1999 Sep 15;7(9):1067-78. PMID:10508780

Page seeded by OCA on Thu Mar 20 13:37:20 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qh3"
Personal tools