3KU9

X-ray structure of the mutant lys300met of polyamine oxidase from zea mays in complex with spermine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0006598	biological_process	polyamine catabolic process
A	0009505	cellular_component	plant-type cell wall
A	0016491	molecular_function	oxidoreductase activity
A	0046208	biological_process	spermine catabolic process
A	0046592	molecular_function	polyamine oxidase activity
A	0048046	cellular_component	apoplast
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0052893	molecular_function	N1-acetylspermine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity
A	0052896	molecular_function	spermidine oxidase (propane-1,3-diamine-forming) activity
A	0052897	molecular_function	N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity
A	0052900	molecular_function	spermine oxidase (propane-1,3-diamine-forming) activity
B	0006598	biological_process	polyamine catabolic process
B	0009505	cellular_component	plant-type cell wall
B	0016491	molecular_function	oxidoreductase activity
B	0046208	biological_process	spermine catabolic process
B	0046592	molecular_function	polyamine oxidase activity
B	0048046	cellular_component	apoplast
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0052893	molecular_function	N1-acetylspermine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity
B	0052896	molecular_function	spermidine oxidase (propane-1,3-diamine-forming) activity
B	0052897	molecular_function	N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity
B	0052900	molecular_function	spermine oxidase (propane-1,3-diamine-forming) activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|PubMed:10368296, ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q, ECO:0007744|PDB:1H82

Chain	Residue	Details
A	GLU430
A	TYR439
B	MET14
B	GLU35
B	ARG43
B	ASN59
B	VAL237
B	TYR399
B	GLU430
B	TYR439
A	MET14
A	GLU35
A	ARG43
A	ASN59
A	VAL237
A	TYR399

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|Ref.10, ECO:0007744|PDB:3KU9, ECO:0007744|PDB:3L1R

Chain	Residue	Details
B	GLU170
B	GLY438
A	GLU62
A	GLU170
A	GLY438
B	GLU62

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site_id	SWS_FT_FI3
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:10368296, ECO:0000269|PubMed:11258887, ECO:0007744|PDB:1B5Q, ECO:0007744|PDB:1H82

Chain	Residue	Details
A	ASN77
B	ASN77

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	1
Details	M-CSA 809

Chain	Residue	Details
A	GLU62	proton acceptor, proton donor

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site_id	MCSA2
Number of Residues	1
Details	M-CSA 809

Chain	Residue	Details
B	GLU62	proton acceptor, proton donor

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