1he5

From Proteopedia

proteopedia linkproteopedia link

spinqualitylabelsall models 1he5, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 [Biliverdin reductase], with EC number [1.3.1.24]. Structure known Active Sites: AC1 and AC2. 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 15:35:01 2007