1fro: Difference between revisions
New page: left|200px<br /> <applet load="1fro" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fro, resolution 2.2Å" /> '''HUMAN GLYOXALASE I W... |
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==About this Structure== | ==About this Structure== | ||
1FRO 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 ZN and GSB as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FRO OCA]]. | 1FRO 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 ZN and GSB as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Lactoylglutathione_lyase Lactoylglutathione lyase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.4.1.5 4.4.1.5]]. Structure known Active Sites: GH1, GH2, GH3, GH4, HD2, HD3, HD4, HD5, ZN1, ZN2, ZN3 and ZN4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FRO OCA]]. | ||
==Reference== | ==Reference== | ||
Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping., Cameron AD, Olin B, Ridderstrom M, Mannervik B, Jones TA, EMBO J. 1997 Jun 16;16(12):3386-95. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9218781 9218781] | Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping., Cameron AD, Olin B, Ridderstrom M, Mannervik B, Jones TA, EMBO J. 1997 Jun 16;16(12):3386-95. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9218781 9218781] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Lactoylglutathione lyase]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cameron, A.D.]] | [[Category: Cameron, A.D.]] | ||
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[[Category: lactoylglutathione lyase]] | [[Category: lactoylglutathione lyase]] | ||
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Revision as of 14:14, 30 October 2007
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HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR
OverviewOverview
The zinc metalloenzyme glyoxalase I catalyses the glutathione-dependent, inactivation of toxic methylglyoxal. The structure of the dimeric human, enzyme in complex with S-benzyl-glutathione has been determined by, multiple isomorphous replacement (MIR) and refined at 2.2 A resolution., Each monomer consists of two domains. Despite only low sequence homology, between them, these domains are structurally equivalent and appear to have, arisen by a gene duplication. On the other hand, there is no structural, homology to the 'glutathione binding domain' found in other, glutathione-linked proteins. 3D domain swapping of the N- and C-terminal, domains has resulted in the active site being situated in the dimer, interface, with the inhibitor and essential zinc ion interacting with side, chains ... [(full description)]
About this StructureAbout this Structure
1FRO is a [Single protein] structure of sequence from [Homo sapiens] with ZN and GSB as [ligands]. Active as [Lactoylglutathione lyase], with EC number [4.4.1.5]. Structure known Active Sites: GH1, GH2, GH3, GH4, HD2, HD3, HD4, HD5, ZN1, ZN2, ZN3 and ZN4. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping., Cameron AD, Olin B, Ridderstrom M, Mannervik B, Jones TA, EMBO J. 1997 Jun 16;16(12):3386-95. PMID:9218781
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