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2atj
From Proteopedia
(New page: 200px<br /> <applet load="2atj" size="450" color="white" frame="true" align="right" spinBox="true" caption="2atj, resolution 2.00Å" /> '''RECOMBINANT HORSERA...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2ATJ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Armoracia_rusticana Armoracia rusticana]] with CA, HEM and BHO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ATJ OCA]]. | + | 2ATJ is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Armoracia_rusticana Armoracia rusticana]] with CA, HEM and BHO as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Peroxidase Peroxidase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.7 1.11.1.7]]. Structure known Active Sites: BEM and BEN. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ATJ OCA]]. |
==Reference== | ==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9609699 9609699] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9609699 9609699] | ||
[[Category: Armoracia rusticana]] | [[Category: Armoracia rusticana]] | ||
| + | [[Category: Peroxidase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gajhede, M.]] | [[Category: Gajhede, M.]] | ||
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[[Category: peroxidase]] | [[Category: peroxidase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:59:30 2007'' |
Revision as of 10:54, 30 October 2007
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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 [Peroxidase], with EC number [1.11.1.7]. Structure known Active Sites: BEM and BEN. 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 Tue Oct 30 12:59:30 2007
Categories: Armoracia rusticana | Peroxidase | Single protein | Gajhede, M. | Henriksen, A. | Schuller, D.J. | BHO | CA | HEM | Oxidoreductase
