1uas Summary


Crystal structure of rice alpha-galactosidase

The structure was published by Fujimoto, Z., Kaneko, S., Momma, M., Kobayashi, H., and Mizuno, H., in 2003 in a paper entitled "Crystal structure of rice alpha-galactosidase complexed with D-galactose" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.5 Å and deposited in 2003.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of alpha-galactosidase. This molecule has the UniProt identifier Q9FXT4 (AGAL_ORYSJ)search. The sample contained 362 residues which is 100% of the natural sequence. Out of 362 residues 362 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A alpha-galactosidase Q9FXT4 (56-417) (AGAL_ORYSJ)search Oryza sativa Japonica Groupsearch 100% 362 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q9FXT4 (56 - 417) alpha-galactosidase Oryza sativa

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (Q9FXT4) alpha-Amylases, C-terminal beta-sheet domainsearch, Amylase, catalytic domainsearch Aldolase class Isearch, Golgi alpha-mannosidase IIsearch PF02065: Melibiasesearch

Chain ID Biological process (GO) Cellular component (GO) Molecular function (GO)
A (Q9FXT4) carbohydrate metabolic processsearch positive regulation of catalytic activitysearch maltose metabolic processsearch metabolic processsearch leaf morphogenesissearch microtubule nucleationsearch starch biosynthetic processsearch positive regulation of flower developmentsearch plant-type cell wallsearch hydrolase activity, acting on glycosyl bondssearch alpha-galactosidase activitysearch hydrolase activity, hydrolyzing O-glycosyl compoundssearch catalytic activitysearch hydrolase activitysearch raffinose alpha-galactosidase activitysearch

Chain InterPro annotation
A Glycoside hydrolase, clan GH-Dsearch Glycoside hydrolase, family 27search Glycosyl hydrolase, family 13, all-betasearch Aldolase-type TIM barrelsearch Glycoside hydrolase superfamilysearch