1he5
From Proteopedia
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|PDB= 1he5 |SIZE=350|CAPTION= <scene name='initialview01'>1he5</scene>, resolution 1.50Å | |PDB= 1he5 |SIZE=350|CAPTION= <scene name='initialview01'>1he5</scene>, resolution 1.50Å | ||
|SITE= <scene name='pdbsite=AC1:Nap+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Lum+Binding+Site+For+Chain+A'>AC2</scene> | |SITE= <scene name='pdbsite=AC1:Nap+Binding+Site+For+Chain+A'>AC1</scene> and <scene name='pdbsite=AC2:Lum+Binding+Site+For+Chain+A'>AC2</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=LUM:LUMICHROME'>LUM</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene> |
| - | |ACTIVITY= [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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1he5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1he5 OCA], [http://www.ebi.ac.uk/pdbsum/1he5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1he5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Pereira, P J.B.]] | [[Category: Pereira, P J.B.]] | ||
[[Category: Perez-Luque, R.]] | [[Category: Perez-Luque, R.]] | ||
| - | [[Category: LUM]] | ||
| - | [[Category: NAP]] | ||
[[Category: alpha/beta dinucleotide binding fold]] | [[Category: alpha/beta dinucleotide binding fold]] | ||
[[Category: biliverdin-ix beta reductase]] | [[Category: biliverdin-ix beta reductase]] | ||
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[[Category: methaemoglobin reductase]] | [[Category: methaemoglobin reductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:03:19 2008'' |
Revision as of 18:03, 30 March 2008
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| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , | ||||||
| Activity: | Biliverdin reductase, with EC number 1.3.1.24 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 single substrate binding site, to which substrates and inhibitors bind primarily through hydrophobic interactions, explaining its broad specificity. The reducible atom of both biliverdin and flavin substrates lies above the reactive C4 of the cofactor, an appropriate position for direct hydride transfer. BVR-B discriminates against the biliverdin IXalpha isomer through steric hindrance at the bilatriene side chain binding pockets. The structure also explains the enzyme's preference for NADP(H) and its B-face stereospecificity.
About this Structure
1HE5 is a Single protein structure of sequence from Homo sapiens. 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 Sun Mar 30 21:03:19 2008
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. | Alpha/beta dinucleotide binding fold | Biliverdin-ix beta reductase | Diaphorase | Flavin reductase | Foetal metabolism | Green haem binding protein | Haem degradation | Methaemoglobin reductase
