1qoz
From Proteopedia
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|PDB= 1qoz |SIZE=350|CAPTION= <scene name='initialview01'>1qoz</scene>, resolution 1.90Å | |PDB= 1qoz |SIZE=350|CAPTION= <scene name='initialview01'>1qoz</scene>, resolution 1.90Å | ||
|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> | |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> | ||
| - | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> | + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene> |
| - | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qoz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qoz OCA], [http://www.ebi.ac.uk/pdbsum/1qoz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qoz RCSB]</span> | ||
}} | }} | ||
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[[Category: Hakulinen, N.]] | [[Category: Hakulinen, N.]] | ||
[[Category: Rouvinen, J.]] | [[Category: Rouvinen, J.]] | ||
| - | [[Category: NAG]] | ||
[[Category: esterase]] | [[Category: esterase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: xylan degradation]] | [[Category: xylan degradation]] | ||
| - | ''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 23:16:56 2008'' |
Revision as of 20:16, 30 March 2008
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| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | and | ||||||
| Ligands: | , | ||||||
| Activity: | Acetylxylan esterase, with EC number 3.1.1.72 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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