3KVE

Structure of native L-amino acid oxidase from Vipera ammodytes ammodytes: stabilization of the quaternary structure by divalent ions and structural changes in the dynamic active site

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001716	molecular_function	L-amino-acid oxidase activity
A	0005576	cellular_component	extracellular region
A	0009063	biological_process	amino acid catabolic process
A	0016491	molecular_function	oxidoreductase activity
B	0001716	molecular_function	L-amino-acid oxidase activity
B	0005576	cellular_component	extracellular region
B	0009063	biological_process	amino acid catabolic process
B	0016491	molecular_function	oxidoreductase activity
C	0001716	molecular_function	L-amino-acid oxidase activity
C	0005576	cellular_component	extracellular region
C	0009063	biological_process	amino acid catabolic process
C	0016491	molecular_function	oxidoreductase activity
D	0001716	molecular_function	L-amino-acid oxidase activity
D	0005576	cellular_component	extracellular region
D	0009063	biological_process	amino acid catabolic process
D	0016491	molecular_function	oxidoreductase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	60
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20938508","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3KVE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P81382","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"20938508","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3KVE","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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