1no3
From Proteopedia
REFINED STRUCTURE OF SOYBEAN LIPOXYGENASE-3 WITH 4-NITROCATECHOL AT 2.15 ANGSTROM RESOLUTION
Overview
4-Nitrocatechol (4NC) is a known inhibitor of lipoxygenase. This work presents the X-ray structure of soybean lipoxygenase-3 in complex with 4NC refined at 2.15 A resolution. The X-ray analysis shows 4NC near iron with partial occupancy, blocking access to Fe but not covalently bound to it. The two hydroxyl groups interact with the C-terminus (4-OH) and His523 ND1 (3-OH). The residues surrounding the iron cofactor, His518*, His523, His709, Ile857* COO(-) and water, form a trigonal bipyramid with the residues marked with asterisks in the axial positions. The water bound to iron and the presence of the inhibitor seem to be responsible for the rearrangements and changes in the geometry of the ligand distribution and confirm the displacement of His518 from iron coordination. A description of the catechol binding contributes to the understanding of lipoxygenase inhibition and the participation of its co-oxidative activity in the utilization of natural flavonoids.
About this Structure
1NO3 is a Single protein structure of sequence from Glycine max. This structure supersedes the now removed PDB entry 1byt. Full crystallographic information is available from OCA.
Reference
Soybean lipoxygenase-3 in complex with 4-nitrocatechol., Skrzypczak-Jankun E, Borbulevych OY, Jankun J, Acta Crystallogr D Biol Crystallogr. 2004 Mar;60(Pt 3):613-5. Epub 2004, Feb 25. PMID:14993710 Page seeded by OCA on Sat May 3 02:46:02 2008
