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1he5
From Proteopedia
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HUMAN BILIVERDIN IX BETA REDUCTASE: NADP/LUMICHROME TERNARY 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
1HE5 is a [Single protein] structure of sequence from [Homo sapiens] with NAP and LUM as [ligands]. Active as [[1]], with EC number [1.3.1.24]. 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 Mon Oct 29 21:04:45 2007
Categories: 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. | LUM | NAP | Alpha/beta dinucleotide binding fold | Biliverdin-ix beta reductase | Diaphorase | Flavin reductase | Foetal metabolism | Green haem binding protein | Haem degradation | Methaemoglobin reductase
