2atj
From Proteopedia
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RECOMBINANT HORSERADISH PEROXIDASE COMPLEX WITH BENZHYDROXAMIC ACID
Overview
The three-dimensional structure of recombinant horseradish peroxidase in, complex with BHA (benzhydroxamic acid) is the first structure of a, peroxidase-substrate complex demonstrating the existence of an aromatic, binding pocket. The crystal structure of the peroxidase-substrate complex, has been determined to 2.0 A resolution with a crystallographic R-factor, of 0.176 (R-free = 0. 192). A well-defined electron density for BHA is, observed in the peroxidase active site, with a hydrophobic pocket, surrounding the aromatic ring of the substrate. The hydrophobic pocket is, provided by residues H42, F68, G69, A140, P141, and F179 and heme C18, C18-methyl, and C20, with the shortest distance (3.7 A) found between heme, C18-methyl and BHA C63. Very little structural rearrangement is seen in, ... [(full description)]
About this Structure
2ATJ is a [Single protein] structure of sequence from [Armoracia rusticana] with CA, HEM and BHO as [ligands]. Active as [[1]], with EC number [1.11.1.7]. Full crystallographic information is available from [OCA].
Reference
Structural interactions between horseradish peroxidase C and the substrate benzhydroxamic acid determined by X-ray crystallography., Henriksen A, Schuller DJ, Meno K, Welinder KG, Smith AT, Gajhede M, Biochemistry. 1998 Jun 2;37(22):8054-60. PMID:9609699
Page seeded by OCA on Mon Oct 29 20:01:04 2007
Categories: Armoracia rusticana | Single protein | Gajhede, M. | Henriksen, A. | Schuller, D.J. | BHO | CA | HEM | Oxidoreductase | Peroxidase
