1F8R

CRYSTAL STRUCTURE OF L-AMINO ACID OXIDASE FROM CALLOSELASMA RHODOSTOMA COMPLEXED WITH CITRATE

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	d1f8ra1	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	FAD-linked reductases, N-terminal domain	L-aminoacid oxidase	(Calloselasma rhodostoma ) [TaxId: 8717 ],	SCOPe (2.08)
A	d1f8ra2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	L-aminoacid/polyamine oxidase	L-aminoacid oxidase	(Calloselasma rhodostoma ) [TaxId: 8717 ],	SCOPe (2.08)
B	d1f8rb1	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	FAD-linked reductases, N-terminal domain	L-aminoacid oxidase	(Calloselasma rhodostoma ) [TaxId: 8717 ],	SCOPe (2.08)
B	d1f8rb2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	L-aminoacid/polyamine oxidase	L-aminoacid oxidase	(Calloselasma rhodostoma ) [TaxId: 8717 ],	SCOPe (2.08)
C	d1f8rc1	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	FAD-linked reductases, N-terminal domain	L-aminoacid oxidase	(Calloselasma rhodostoma ) [TaxId: 8717 ],	SCOPe (2.08)
C	d1f8rc2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	L-aminoacid/polyamine oxidase	L-aminoacid oxidase	(Calloselasma rhodostoma ) [TaxId: 8717 ],	SCOPe (2.08)
D	d1f8rd1	Alpha and beta proteins (a/b)	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	FAD-linked reductases, N-terminal domain	L-aminoacid oxidase	(Calloselasma rhodostoma ) [TaxId: 8717 ],	SCOPe (2.08)
D	d1f8rd2	Alpha and beta proteins (a+b)	FAD-linked reductases, C-terminal domain	FAD-linked reductases, C-terminal domain	L-aminoacid/polyamine oxidase	L-aminoacid oxidase	(Calloselasma rhodostoma ) [TaxId: 8717 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Flavoreductase-like	8057758	3000055	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Flavoreductase-like	8057758	3000055	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Flavoreductase-like	8057758	3000055	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Flavoreductase-like	8057758	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_2	e1f8rA1	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_2	ECOD (1.6)
A	Amino_oxidase_1st	e1f8rA2	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_2	e1f8rB1	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_2	ECOD (1.6)
B	Amino_oxidase_1st	e1f8rB2	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_2	e1f8rC1	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_2	ECOD (1.6)
C	Amino_oxidase_1st	e1f8rC2	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)
D	Amino_oxidase_2nd_2	e1f8rD1	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_2	ECOD (1.6)
D	Amino_oxidase_1st	e1f8rD2	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	3.90.660.10	Alpha Beta	Alpha-Beta Complex	Polyamine Oxidase	Chain A, domain 2	CATH (4.3.0)
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	1.10.405.10	Mainly Alpha	Orthogonal Bundle	Guanine Nucleotide Dissociation Inhibitor	domain 1	CATH (4.3.0)
B	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	1.10.405.10	Mainly Alpha	Orthogonal Bundle	Guanine Nucleotide Dissociation Inhibitor	domain 1	CATH (4.3.0)
C	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	1.10.405.10	Mainly Alpha	Orthogonal Bundle	Guanine Nucleotide Dissociation Inhibitor	domain 1	CATH (4.3.0)
D	3.90.660.10	Alpha Beta	Alpha-Beta Complex	Polyamine Oxidase	Chain A, domain 2	CATH (4.3.0)
D	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
D	1.10.405.10	Mainly Alpha	Orthogonal Bundle	Guanine Nucleotide Dissociation Inhibitor	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	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, D	L-AMINO ACID OXIDASE	oxidoreductase activity, acting on the CH-NH2 group of donors oxidoreductase activity oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor L-phenylalaine oxidase activity primary methylamine oxidase activity catalytic activity L-amino-acid oxidase activity toxin activity	cellular process apoptotic process cell death programmed cell death catabolic process metabolic process amino acid metabolic process primary metabolic process amino acid catabolic process biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to external stimulus cellular process apoptotic process cell death programmed cell death catabolic process metabolic process amino acid metabolic process primary metabolic process amino acid catabolic process biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response response to external stimulus response to biotic stimulus defense response to bacterium defense response to other organism response to stress response to bacterium response to external biotic stimulus disruption of cell in another organism disruption of anatomical structure in another organism killing of cells of another organism cell killing	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

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

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

Chains	Enzyme Name	Description	Catalytic Residues
A	L-amino-acid oxidase M-CSA #555	L-aminoacid oxidase is a dimeric flavoprotein. it uses a non-covalently bound FAD cofactor in catalysing the stereospecific oxidative deamination of an L-amino acid substrate to an alpha ketoacid, forming ammonia and hydrogen peroxide. The enzyme shows a marked preference for hydrophobic amino acids including phenylalanine, tryptophan, tyrosine and leucine.	Defined by 2 residues: HIS:A-223LYS:A-326 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.4.3.2 (PDB Primary Data) Search M-CSA Motif + EC 1.4.3.2

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.