1hsz

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[[Image:1hsz.gif|left|200px]]<br /><applet load="1hsz" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hsz.gif|left|200px]]
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caption="1hsz, resolution 2.20&Aring;" />
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'''HUMAN BETA-1 ALCOHOL DEHYDROGENASE (ADH1B*1)'''<br />
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{{Structure
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|PDB= 1hsz |SIZE=350|CAPTION= <scene name='initialview01'>1hsz</scene>, resolution 2.20&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1]
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|GENE= ADH2 OR ADH1B*1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''HUMAN BETA-1 ALCOHOL DEHYDROGENASE (ADH1B*1)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1HSZ 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=PO4:'>PO4</scene> and <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Alcohol_dehydrogenase Alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.1 1.1.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HSZ OCA].
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1HSZ 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=1HSZ OCA].
==Reference==
==Reference==
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Three-dimensional structures of the three human class I alcohol dehydrogenases., Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD, Protein Sci. 2001 Apr;10(4):697-706. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11274460 11274460]
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Three-dimensional structures of the three human class I alcohol dehydrogenases., Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD, Protein Sci. 2001 Apr;10(4):697-706. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11274460 11274460]
[[Category: Alcohol dehydrogenase]]
[[Category: Alcohol dehydrogenase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: zinc]]
[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:04:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:41:10 2008''

Revision as of 09:41, 20 March 2008

Image:1hsz.gif


PDB ID 1hsz

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: , and
Gene: ADH2 OR ADH1B*1 (Homo sapiens)
Activity: Alcohol dehydrogenase, with EC number 1.1.1.1
Coordinates: save as pdb, mmCIF, xml



HUMAN BETA-1 ALCOHOL DEHYDROGENASE (ADH1B*1)


Contents

Overview

In contrast with other animal species, humans possess three distinct genes for class I alcohol dehydrogenase and show polymorphic variation in the ADH1B and ADH1C genes. The three class I alcohol dehydrogenase isoenzymes share approximately 93% sequence identity but differ in their substrate specificity and their developmental expression. We report here the first three-dimensional structures for the ADH1A and ADH1C*2 gene products at 2.5 and 2.0 A, respectively, and the structure of the ADH1B*1 gene product in a binary complex with cofactor at 2.2 A. Not surprisingly, the overall structure of each isoenzyme is highly similar to the others. However, the substitution of Gly for Arg at position 47 in the ADH1A isoenzyme promotes a greater extent of domain closure in the ADH1A isoenzyme, whereas substitution at position 271 may account for the lower turnover rate for the ADH1C*2 isoenzyme relative to its polymorphic variant, ADH1C*1. The substrate-binding pockets of each isoenzyme possess a unique topology that dictates each isoenzyme's distinct but overlapping substrate preferences. ADH1*B1 has the most restrictive substrate-binding site near the catalytic zinc atom, whereas both ADH1A and ADH1C*2 possess amino acid substitutions that correlate with their better efficiency for the oxidation of secondary alcohols. These structures describe the nature of their individual substrate-binding pockets and will improve our understanding of how the metabolism of beverage ethanol affects the normal metabolic processes performed by these isoenzymes.

Disease

Known diseases associated with this structure: Alcoholism, susceptibility to OMIM:[103720]

About this Structure

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

Reference

Three-dimensional structures of the three human class I alcohol dehydrogenases., Niederhut MS, Gibbons BJ, Perez-Miller S, Hurley TD, Protein Sci. 2001 Apr;10(4):697-706. PMID:11274460

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