1hdo
From Proteopedia
(New page: 200px<br /> <applet load="1hdo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hdo, resolution 1.15Å" /> '''HUMAN BILIVERDIN IX...) |
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==About this Structure== | ==About this Structure== | ||
- | 1HDO 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 NAP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.24 1.3.1.24]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HDO OCA]]. | + | 1HDO 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 NAP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Biliverdin_reductase Biliverdin reductase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.24 1.3.1.24]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HDO OCA]]. |
==Reference== | ==Reference== | ||
Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme., Pereira PJ, Macedo-Ribeiro S, Parraga A, Perez-Luque R, Cunningham O, Darcy K, Mantle TJ, Coll M, Nat Struct Biol. 2001 Mar;8(3):215-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11224564 11224564] | Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme., Pereira PJ, Macedo-Ribeiro S, Parraga A, Perez-Luque R, Cunningham O, Darcy K, Mantle TJ, Coll M, Nat Struct Biol. 2001 Mar;8(3):215-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11224564 11224564] | ||
+ | [[Category: Biliverdin reductase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: methaemoglobin reductase]] | [[Category: methaemoglobin reductase]] | ||
- | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:02:49 2007'' |
Revision as of 11:58, 30 October 2007
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HUMAN BILIVERDIN IX BETA REDUCTASE: NADP COMPLEX
Overview
Biliverdin IXbeta reductase (BVR-B) catalyzes the pyridine, nucleotide-dependent production of bilirubin-IXbeta, the major heme, catabolite during early fetal development. BVR-B displays a preference for, biliverdin isomers without propionates straddling the C10 position, in, contrast to biliverdin IXalpha reductase (BVR-A), the major form of BVR in, adult human liver. In addition to its tetrapyrrole clearance role in the, fetus, BVR-B has flavin and ferric reductase activities in the adult. We, have solved the structure of human BVR-B in complex with NADP+ at 1.15 A, resolution. Human BVR-B is a monomer displaying an alpha/beta dinucleotide, binding fold. The structures of ternary complexes with mesobiliverdin, IValpha, biliverdin IXalpha, FMN and lumichrome show that human BVR-B has, a ... [(full description)]
About this Structure
1HDO is a [Single protein] structure of sequence from [Homo sapiens] with NAP as [ligand]. Active as [Biliverdin reductase], with EC number [1.3.1.24]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structure of human biliverdin IXbeta reductase, an early fetal bilirubin IXbeta producing enzyme., Pereira PJ, Macedo-Ribeiro S, Parraga A, Perez-Luque R, Cunningham O, Darcy K, Mantle TJ, Coll M, Nat Struct Biol. 2001 Mar;8(3):215-20. PMID:11224564
Page seeded by OCA on Tue Oct 30 14:02:49 2007
Categories: Biliverdin reductase | Homo sapiens | Single protein | Coll, M. | Cunningham, O. | Darcy, K. | Macedo-Ribeiro, S. | Mantle, T.J. | Parraga, A. | Pereira, P.J.B. | Perez-Luque, R. | NAP | Alpha/beta dinucleotide binding fold | Biliverdin-ix beta reductase | Diaphorase | Flavin reductase | Foetal metabolism | Green haem binding protein | Haem degradation | Methaemoglobin reductase