Structure of PDB 1uas Chain A

Receptor sequence
>1uasA (length=362) Species: 4530 (Oryza sativa) [Search protein sequence]
FENGLGRTPQMGWNSWNHFYCGINEQIIRETADALVNTGLAKLGYQYVNI
DDCWAEYSRDSQGNFVPNRQTFPSGIKALADYVHAKGLKLGIYSDAGSQT
CSNKMPGSLDHEEQDVKTFASWGVDYLKYDNCNDAGRSVMERYTRMSNAM
KTYGKNIFFSLCEWGKENPATWAGRMGNSWRTTGDIADNWGSMTSRADEN
DQWAAYAGPGGWNDPDMLEVGNGGMSEAEYRSHFSIWALAKAPLLIGCDV
RSMSQQTKNILSNSEVIAVNQDSLGVQGKKVQSDNGLEVWAGPLSNNRKA
VVLWNRQSYQATITAHWSNIGLAGSVAVTARDLWAHSSFAAQGQISASVA
PHDCKMYVLTPN
3D structure
PDB1uas Crystal structure of rice alpha-galactosidase complexed with D-galactose
ChainA
Resolution1.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D130 D185
Catalytic site (residue number reindexed from 1) D130 D185
Enzyme Commision number 3.2.1.22: alpha-galactosidase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GLA A W16 D51 D52 C101 K128 D130 C162 W164 R181 D185 W16 D51 D52 C101 K128 D130 C162 W164 R181 D185
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0004557 alpha-galactosidase activity
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0052692 raffinose alpha-galactosidase activity
Biological Process
GO:0000272 polysaccharide catabolic process
GO:0005975 carbohydrate metabolic process
GO:0009620 response to fungus
GO:0009911 positive regulation of flower development
GO:0009965 leaf morphogenesis
GO:0051682 galactomannan catabolic process
Cellular Component
GO:0009505 plant-type cell wall
GO:0048046 apoplast

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1uas, PDBe:1uas, PDBj:1uas
PDBsum1uas
PubMed12657636
UniProtQ9FXT4|AGAL_ORYSJ Alpha-galactosidase (Gene Name=Os10g0493600)

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