1uas
From Proteopedia
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|PDB= 1uas |SIZE=350|CAPTION= <scene name='initialview01'>1uas</scene>, resolution 1.50Å | |PDB= 1uas |SIZE=350|CAPTION= <scene name='initialview01'>1uas</scene>, resolution 1.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Alpha-galactosidase Alpha-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.22 3.2.1.22] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Alpha-galactosidase Alpha-galactosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.22 3.2.1.22] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uas FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uas OCA], [http://www.ebi.ac.uk/pdbsum/1uas PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1uas RCSB]</span> | ||
}} | }} | ||
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[[Category: Mizuno, H.]] | [[Category: Mizuno, H.]] | ||
[[Category: Momma, M.]] | [[Category: Momma, M.]] | ||
| - | [[Category: GLA]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: PT]] | ||
| - | [[Category: SO4]] | ||
[[Category: beta-alpha-barrel]] | [[Category: beta-alpha-barrel]] | ||
[[Category: greek key motif]] | [[Category: greek key motif]] | ||
[[Category: tim-barrel]] | [[Category: tim-barrel]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:07:41 2008'' |
Revision as of 21:07, 30 March 2008
| |||||||
| , resolution 1.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Alpha-galactosidase, with EC number 3.2.1.22 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of rice alpha-galactosidase
Overview
alpha-Galactosidases catalyze the hydrolysis of alpha-1,6-linked galactosyl residues from galacto-oligosaccharides and polymeric galacto-(gluco)mannans. The crystal structure of rice alpha-galactosidase has been determined at 1.5A resolution using the multiple isomorphous replacement method. The structure consisted of a catalytic domain and a C-terminal domain and was essentially the same as that of alpha-N-acetylgalactosaminidase, which is the same member of glycosyl hydrolase family 27. The catalytic domain had a (beta/alpha)8-barrel structure, and the C-terminal domain was made up of eight beta-strands containing a Greek key motif. The structure was solved as a complex with d-galactose, providing a mode of substrate binding in detail. The d-galactose molecule was found bound in the active site pocket on the C-terminal side of the central beta-barrel of the catalytic domain. The d-galactose molecule consisted of a mixture of two anomers present in a ratio equal to their natural abundance. Structural comparisons of rice alpha-galactosidase with chicken alpha-N-acetylgalactosaminidase provided further understanding of the substrate recognition mechanism in these enzymes.
About this Structure
1UAS is a Single protein structure of sequence from Oryza sativa. Full crystallographic information is available from OCA.
Reference
Crystal structure of rice alpha-galactosidase complexed with D-galactose., Fujimoto Z, Kaneko S, Momma M, Kobayashi H, Mizuno H, J Biol Chem. 2003 May 30;278(22):20313-8. Epub 2003 Mar 25. PMID:12657636
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