1B5Q

A 30 ANGSTROM U-SHAPED CATALYTIC TUNNEL IN THE CRYSTAL STRUCTURE OF POLYAMINE OXIDASE

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1b5qa1	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	FAD-linked reductases, N-terminal domain	Polyamine oxidase	(Zea mays ) [TaxId: 4577 ],	SCOPe (2.08)
A	d1b5qa2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	L-aminoacid/polyamine oxidase	Polyamine oxidase	(Zea mays ) [TaxId: 4577 ],	SCOPe (2.08)
C	d1b5qc1	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	FAD-linked reductases, N-terminal domain	Polyamine oxidase	(Zea mays ) [TaxId: 4577 ],	SCOPe (2.08)
C	d1b5qc2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	L-aminoacid/polyamine oxidase	Polyamine oxidase	(Zea mays ) [TaxId: 4577 ],	SCOPe (2.08)
B	d1b5qb1	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	FAD-linked reductases, N-terminal domain	Polyamine oxidase	(Zea mays ) [TaxId: 4577 ],	SCOPe (2.08)
B	d1b5qb2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	L-aminoacid/polyamine oxidase	Polyamine oxidase	(Zea mays ) [TaxId: 4577 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Amine oxidase-like	8057746	4000128	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Flavoreductase-like	8057747	3000055	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	Flavoreductase-like	8057747	3000055	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Flavoreductase-like	8057747	3000055	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Amino_oxidase_2nd	e1b5qA1	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: Amino_oxidase_2nd	ECOD (1.6)
A	Amino_oxidase_1st	e1b5qA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: Amino_oxidase_1st	ECOD (1.6)
C	Amino_oxidase_2nd	e1b5qC1	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: Amino_oxidase_2nd	ECOD (1.6)
C	Amino_oxidase_1st	e1b5qC2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: Amino_oxidase_1st	ECOD (1.6)
B	Amino_oxidase_2nd	e1b5qB1	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD-linked reductases-C (From Topology)	T: FAD-linked reductases-C	F: Amino_oxidase_2nd	ECOD (1.6)
B	Amino_oxidase_1st	e1b5qB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: Amino_oxidase_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
A	3.90.660.10	Alpha Beta	Alpha-Beta Complex	Polyamine Oxidase	Chain A, domain 2	CATH (4.3.0)
C	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
C	3.90.660.10	Alpha Beta	Alpha-Beta Complex	Polyamine Oxidase	Chain A, domain 2	CATH (4.3.0)
B	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
B	3.90.660.10	Alpha Beta	Alpha-Beta Complex	Polyamine Oxidase	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF01593	Flavin containing amine oxidoreductase (Amino_oxidase)	Flavin containing amine oxidoreductase	This family consists of various amine oxidases, including maze polyamine oxidase (PAO) [1] and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene ...	This family consists of various amine oxidases, including maze polyamine oxidase (PAO) [1] and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines [2]. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium [3]. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines [1]. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	PROTEIN (POLYAMINE OXIDASE)	oxidoreductase activity catalytic activity oxidoreductase activity, acting on the CH-NH group of donors, oxygen as acceptor polyamine oxidase activity spermine oxidase (propane-1,3-diamine-forming) activity oxidoreductase activity, acting on the CH-NH group of donors flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding oxidoreductase activity catalytic activity oxidoreductase activity, acting on the CH-NH group of donors, oxygen as acceptor polyamine oxidase activity spermine oxidase (propane-1,3-diamine-forming) activity oxidoreductase activity, acting on the CH-NH group of donors flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding N8-acetylspermidine:oxygen oxidoreductase (propane-1,3-diamine-forming) activity	amine metabolic process catabolic process metabolic process cellular process polyamine catabolic process polyamine metabolic process biogenic amine catabolic process biogenic amine metabolic process amine catabolic process spermine catabolic process spermine metabolic process	cellular anatomical structure extracellular region apoplast cell periphery external encapsulating structure plant-type cell wall cell wall

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR002937	Amine oxidase	Domain
A, B, C	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A, B, C	IPR001613	Flavin amine oxidase	Family
A, B, C	IPR050281	Flavin monoamine oxidase and related enzymes	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
C	polyamine oxidase (propane-1,3-diamine-forming) M-CSA #809	Polyamine oxidase is able to catalyse the oxidation of the secondary amino groups of polyamines to their corresponding imino forms, using FAD as a cofactor coupled to eventual reduction of H2O2 to form water. The product of the reaction depends on the initial starting material; for example mammalian polyamine oxidase can convert spermidine to putrescine. Polyamines bind DNA and regulate transcription and translation, thus play roles in cell differentiation and multiplication, causing them to be implicated in the development of certain forms of cancer. As a result the enzyme is of interest as a drug target. Despite different physiological roles, mammalian, plant and bacterial forms of the enzyme show significant sequence and structural homology, and polyamine oxidases also show homology to monoamine oxidases, suggesting a common catalytic mechanism.	Defined by 1 residue: GLU:C-62 \| Explore in 3D: M-CSA Motif Definition At least 2 residues must be present to support Structure Motif searching. EC: 1.5.3.14 (UniProt) EC: 1.5.3.15 (UniProt)

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.