1RSG

Crystal structure of the polyamine oxidase Fms1 from yeast

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003682	molecular_function	chromatin binding
A	0005737	cellular_component	cytoplasm
A	0006338	biological_process	chromatin remodeling
A	0015940	biological_process	pantothenate biosynthetic process
A	0016491	molecular_function	oxidoreductase activity
A	0046208	biological_process	spermine catabolic process
A	0046592	molecular_function	polyamine oxidase activity
A	0050660	molecular_function	flavin adenine dinucleotide binding
A	0052897	molecular_function	N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity
A	0052901	molecular_function	spermine:oxygen oxidoreductase (spermidine-forming) activity
A	0052902	molecular_function	spermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity
A	0052903	molecular_function	N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity
A	0052904	molecular_function	N1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity
B	0003682	molecular_function	chromatin binding
B	0005737	cellular_component	cytoplasm
B	0006338	biological_process	chromatin remodeling
B	0015940	biological_process	pantothenate biosynthetic process
B	0016491	molecular_function	oxidoreductase activity
B	0046208	biological_process	spermine catabolic process
B	0046592	molecular_function	polyamine oxidase activity
B	0050660	molecular_function	flavin adenine dinucleotide binding
B	0052897	molecular_function	N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity
B	0052901	molecular_function	spermine:oxygen oxidoreductase (spermidine-forming) activity
B	0052902	molecular_function	spermidine:oxygen oxidoreductase (3-aminopropanal-forming) activity
B	0052903	molecular_function	N1-acetylspermine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity
B	0052904	molecular_function	N1-acetylspermidine:oxygen oxidoreductase (3-acetamidopropanal-forming) activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	38
Details	BINDING SITE FOR RESIDUE FAD A 1801

Chain	Residue
A	GLY15
A	ARG47
A	GLY62
A	ALA63
A	SER64
A	TRP65
A	HIS67
A	CYS221
A	VAL223
A	THR252
A	VAL253
A	GLY17
A	PRO254
A	GLY270
A	LEU294
A	LYS296
A	TRP440
A	TYR445
A	GLY478
A	GLU479
A	GLY487
A	CYS488
A	ILE18
A	ALA489
A	ALA492
A	HOH1802
A	HOH1805
A	HOH1808
A	HOH1810
A	HOH1815
A	HOH1836
A	HOH2168
A	ALA19
A	GLU39
A	ALA40
A	ARG41
A	GLY45
A	GLY46

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site_id	AC2
Number of Residues	36
Details	BINDING SITE FOR RESIDUE FAD B 1802

Chain	Residue
B	GLY15
B	GLY17
B	ILE18
B	ALA19
B	LEU38
B	GLU39
B	ALA40
B	ARG41
B	GLY45
B	GLY46
B	ARG47
B	GLY62
B	ALA63
B	SER64
B	TRP65
B	HIS67
B	CYS221
B	VAL223
B	THR252
B	VAL253
B	GLY270
B	LEU294
B	TYR445
B	GLY478
B	GLU479
B	GLY487
B	CYS488
B	ALA489
B	ALA492
B	HOH1808
B	HOH1821
B	HOH1822
B	HOH1838
B	HOH1868
B	HOH1905
B	HOH2032

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1f8r

Chain	Residue	Details
A	GLY193
A	LYS296

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1f8r

Chain	Residue	Details
B	GLY193
B	LYS296

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site_id	CSA3
Number of Residues	1
Details	Annotated By Reference To The Literature 1f8r

Chain	Residue	Details
A	HIS67

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site_id	CSA4
Number of Residues	1
Details	Annotated By Reference To The Literature 1f8r

Chain	Residue	Details
B	HIS67

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