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1FA2

CRYSTAL STRUCTURE OF BETA-AMYLASE FROM SWEET POTATO

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0016161molecular_functionbeta-amylase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PROSITE/UniProt
site_idPS00506
Number of Residues9
DetailsBETA_AMYLASE_1 Beta-amylase active site 1. HqCGGNVGD
ChainResidueDetails
AHIS94-ASP102

site_idPS00679
Number of Residues11
DetailsBETA_AMYLASE_2 Beta-amylase active site 2. GaAGELRYPSY
ChainResidueDetails
AGLY183-TYR193

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10050","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P10538","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P10538","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1bya
ChainResidueDetails
AASP102
AGLU187

239492

PDB entries from 2025-07-30

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