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1UAS

Crystal structure of rice alpha-galactosidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004557molecular_functionalpha-galactosidase activity
A0005975biological_processcarbohydrate metabolic process
A0009505cellular_componentplant-type cell wall
A0009620biological_processresponse to fungus
A0009911biological_processpositive regulation of flower development
A0009965biological_processleaf morphogenesis
A0015925molecular_functiongalactosidase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0048046cellular_componentapoplast
A0051682biological_processgalactomannan catabolic process
A0052692molecular_functionraffinose alpha-galactosidase activity
Functional Information from PROSITE/UniProt
site_idPS00512
Number of Residues17
DetailsALPHA_GALACTOSIDASE Alpha-galactosidase signature. GYqyVnIDDc.Waeys...RD
ChainResidueDetails
AGLY44-ASP60

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:12657636
ChainResidueDetails
AASP130

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:12657636
ChainResidueDetails
AASP185

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:12657636
ChainResidueDetails
ATRP16
AASP51
AASP52
ACYS101
ALYS128
AASP130
ATRP164
AARG181
AASP185

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 12005440, 12657636
ChainResidueDetails
AASP185
AASP130

site_idMCSA1
Number of Residues2
DetailsM-CSA 913
ChainResidueDetails
AASP130covalent catalysis
AASP185proton shuttle (general acid/base)

222036

PDB entries from 2024-07-03

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