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3VX0

Crystal Structure of alpha-amylase from Aspergillus oryzae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004556molecular_functionalpha-amylase activity
A0005509molecular_functioncalcium ion binding
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0009277cellular_componentfungal-type cell wall
A0016052biological_processcarbohydrate catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030287cellular_componentcell wall-bounded periplasmic space
A0030428cellular_componentcell septum
A0031521cellular_componentspitzenkorper
A0032163cellular_componenthyphal septin band
A0043169molecular_functioncation binding
A0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"9283074","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"9283074","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9283074","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16880540","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"6609921","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9283074","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9283074","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"9283074","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000125","evidences":[{"source":"PubMed","id":"16880540","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-11-05

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