1qoz

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[[Image:1qoz.gif|left|200px]]<br /><applet load="1qoz" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qoz.gif|left|200px]]
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caption="1qoz, resolution 1.90&Aring;" />
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'''CATALYTIC CORE DOMAIN OF ACETYL XYLAN ESTERASE FROM TRICHODERMA REESEI'''<br />
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{{Structure
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|PDB= 1qoz |SIZE=350|CAPTION= <scene name='initialview01'>1qoz</scene>, resolution 1.90&Aring;
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|SITE= <scene name='pdbsite=AS1:Active+Site+Catalytic+Triad+(Chain+A)'>AS1</scene> and <scene name='pdbsite=AS2:Active+Site+Catalytic+Triad+(Chain+B)'>AS2</scene>
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Acetylxylan_esterase Acetylxylan esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.72 3.1.1.72]
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|GENE=
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}}
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'''CATALYTIC CORE DOMAIN OF ACETYL XYLAN ESTERASE FROM TRICHODERMA REESEI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1QOZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Acetylxylan_esterase Acetylxylan esterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.72 3.1.1.72] Known structural/functional Sites: <scene name='pdbsite=AS1:Active+Site+Catalytic+Triad+(Chain+A)'>AS1</scene> and <scene name='pdbsite=AS2:Active+Site+Catalytic+Triad+(Chain+B)'>AS2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOZ OCA].
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1QOZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Hypocrea_jecorina Hypocrea jecorina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QOZ OCA].
==Reference==
==Reference==
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Crystallization and preliminary X-ray diffraction studies of the catalytic core of acetyl xylan esterase from Trichoderma reesei., Hakulinen N, Tenkanen M, Rouvinen J, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):430-2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9761918 9761918]
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Crystallization and preliminary X-ray diffraction studies of the catalytic core of acetyl xylan esterase from Trichoderma reesei., Hakulinen N, Tenkanen M, Rouvinen J, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):430-2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9761918 9761918]
[[Category: Acetylxylan esterase]]
[[Category: Acetylxylan esterase]]
[[Category: Hypocrea jecorina]]
[[Category: Hypocrea jecorina]]
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[[Category: xylan degradation]]
[[Category: xylan degradation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:42:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:40:43 2008''

Revision as of 11:40, 20 March 2008


PDB ID 1qoz

Drag the structure with the mouse to rotate
, resolution 1.90Å
Sites: and
Ligands:
Activity: Acetylxylan esterase, with EC number 3.1.1.72
Coordinates: save as pdb, mmCIF, xml



CATALYTIC CORE DOMAIN OF ACETYL XYLAN ESTERASE FROM TRICHODERMA REESEI


Overview

Acetyl xylan esterase is involved in the biodegradation of hemicellulose. It cleaves O-acetyl groups from xylan, which is the most abundant hemicellulose in nature. The catalytic core of acetyl xylan esterase from T. reesei has been crystallized and X-ray diffraction data at 2.3 A collected. The crystal belongs to the triclinic space group P1 with unit-cell parameters a = 50.3, b = 62. 1, c = 40.0 A, alpha = 110.1, beta = 113.6 and gamma = 97.9 degrees. The asymmetric unit contains two molecules.

About this Structure

1QOZ is a Single protein structure of sequence from Hypocrea jecorina. Full crystallographic information is available from OCA.

Reference

Crystallization and preliminary X-ray diffraction studies of the catalytic core of acetyl xylan esterase from Trichoderma reesei., Hakulinen N, Tenkanen M, Rouvinen J, Acta Crystallogr D Biol Crystallogr. 1998 May 1;54(Pt 3):430-2. PMID:9761918

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