1OAC

CRYSTAL STRUCTURE OF A QUINOENZYME: COPPER AMINE OXIDASE OF ESCHERICHIA COLI AT 2 ANGSTROEMS RESOLUTION

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
Protein Modification Annotation
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	d1oaca1	All beta proteins	Supersandwich	Amine oxidase catalytic domain	Amine oxidase catalytic domain	Copper amine oxidase, domain 3	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1oaca2	Alpha and beta proteins (a+b)	Cystatin-like	Amine oxidase N-terminal region	Amine oxidase N-terminal region	Copper amine oxidase, domains 1 and 2	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d1oaca4	Alpha and beta proteins (a+b)	N domain of copper amine oxidase-like	Copper amine oxidase, domain N	Copper amine oxidase, domain N	Copper amine oxidase, domain N	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1oacb1	All beta proteins	Supersandwich	Amine oxidase catalytic domain	Amine oxidase catalytic domain	Copper amine oxidase, domain 3	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1oacb2	Alpha and beta proteins (a+b)	Cystatin-like	Amine oxidase N-terminal region	Amine oxidase N-terminal region	Copper amine oxidase, domains 1 and 2	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1oacb4	Alpha and beta proteins (a+b)	N domain of copper amine oxidase-like	Copper amine oxidase, domain N	Copper amine oxidase, domain N	Copper amine oxidase, domain N	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Amine oxidase N-terminal region	8034642	3000455	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Amine oxidase N-terminal region	8034641	3000455	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	amine oxidase catalytic domain	8041516	3001726	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Copper amine oxidase, domain N	8035163	3001833	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Amine oxidase N-terminal region	8034641	3000455	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Copper amine oxidase, domain N	8035163	3001833	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	amine oxidase catalytic domain	8041516	3001726	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Amine oxidase N-terminal region	8034642	3000455	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	Cu_amine_oxid	e1oacA1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Cu_amine_oxid	ECOD (1.6)
A	Cu_amine_oxidN1	e1oacA4	A: a+b two layers	X: Type III secretory system chaperone-like	H: N domain of copper amine oxidase (From Topology)	T: N domain of copper amine oxidase	F: Cu_amine_oxidN1	ECOD (1.6)
A	Cu_amine_oxidN2	e1oacA2	A: a+b two layers	X: Cystatin-like	H: Amine oxidase N-terminal region (From Topology)	T: Amine oxidase N-terminal region	F: Cu_amine_oxidN2	ECOD (1.6)
A	Cu_amine_oxidN3	e1oacA3	A: a+b two layers	X: Cystatin-like	H: Amine oxidase N-terminal region (From Topology)	T: Amine oxidase N-terminal region	F: Cu_amine_oxidN3	ECOD (1.6)
B	Cu_amine_oxid	e1oacB1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Cu_amine_oxid	ECOD (1.6)
B	Cu_amine_oxidN1	e1oacB4	A: a+b two layers	X: Type III secretory system chaperone-like	H: N domain of copper amine oxidase (From Topology)	T: N domain of copper amine oxidase	F: Cu_amine_oxidN1	ECOD (1.6)
B	Cu_amine_oxidN2	e1oacB2	A: a+b two layers	X: Cystatin-like	H: Amine oxidase N-terminal region (From Topology)	T: Amine oxidase N-terminal region	F: Cu_amine_oxidN2	ECOD (1.6)
B	Cu_amine_oxidN3	e1oacB3	A: a+b two layers	X: Cystatin-like	H: Amine oxidase N-terminal region (From Topology)	T: Amine oxidase N-terminal region	F: Cu_amine_oxidN3	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.457.10	Alpha Beta	2-Layer Sandwich	Copper Amine Oxidase	Chain A, domain 1	CATH (4.3.0)
A	3.10.450.40	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
A	2.70.98.20	Mainly Beta	Distorted Sandwich	Beta-galactosidase	Chain A, domain 5	CATH (4.3.0)
B	3.30.457.10	Alpha Beta	2-Layer Sandwich	Copper Amine Oxidase	Chain A, domain 1	CATH (4.3.0)
B	3.10.450.40	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
B	2.70.98.20	Mainly Beta	Distorted Sandwich	Beta-galactosidase	Chain A, domain 5	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02728	Copper amine oxidase, N3 domain (Cu_amine_oxidN3)	Copper amine oxidase, N3 domain	This domain is the second or third structural domain in copper amine oxidases, it is known as the N3 domain. Its function is uncertain. The catalytic domain can be found in Pfam:PF01179. Copper amine oxidases are a ubiquitous and novel group of quino ...	This domain is the second or third structural domain in copper amine oxidases, it is known as the N3 domain. Its function is uncertain. The catalytic domain can be found in Pfam:PF01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyse the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).	Domain
A, B	PF02727	Copper amine oxidase, N2 domain (Cu_amine_oxidN2)	Copper amine oxidase, N2 domain	This domain is the first or second structural domain in copper amine oxidases, it is known as the N2 domain. Its function is uncertain. The catalytic domain can be found in Pfam:PF01179. Copper amine oxidases are a ubiquitous and novel group of quino ...	This domain is the first or second structural domain in copper amine oxidases, it is known as the N2 domain. Its function is uncertain. The catalytic domain can be found in Pfam:PF01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyse the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).	Domain
A, B	PF01179	Copper amine oxidase, enzyme domain (Cu_amine_oxid)	Copper amine oxidase, enzyme domain	Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyse the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dime ...	Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyse the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ). This family corresponds to the catalytic domain of the enzyme.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	COPPER AMINE OXIDASE	aliphatic amine oxidase activity 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 catalytic activity aliphatic amine dehydrogenase activity cation binding ion binding binding calcium ion binding metal ion binding small molecule binding quinone binding transition metal ion binding aliphatic amine oxidase activity 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 catalytic activity aliphatic amine dehydrogenase activity cation binding ion binding binding calcium ion binding metal ion binding small molecule binding quinone binding transition metal ion binding copper ion binding primary methylamine oxidase activity	catabolic process oxoacid metabolic process aromatic amino acid family catabolic process amino acid metabolic process organic acid catabolic process organic acid metabolic process alpha-amino acid metabolic process cellular catabolic process carboxylic acid catabolic process small molecule metabolic process amino acid catabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process L-phenylalanine catabolic process aromatic amino acid metabolic process catabolic process oxoacid metabolic process aromatic amino acid family catabolic process amino acid metabolic process organic acid catabolic process organic acid metabolic process alpha-amino acid metabolic process cellular catabolic process carboxylic acid catabolic process small molecule metabolic process amino acid catabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process L-phenylalanine catabolic process aromatic amino acid metabolic process cellular metabolic process carboxylic acid metabolic process L-amino acid catabolic process primary metabolic process L-amino acid metabolic process L-phenylalanine metabolic process proteinogenic amino acid metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid catabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process metabolic process cellular process small molecule catabolic process phenylethylamine catabolic process amine metabolic process phenylethylamine metabolic process primary amino compound catabolic process cellular biogenic amine catabolic process primary amino compound metabolic process biogenic amine metabolic process amine catabolic process	periplasmic space cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR000269	Copper amine oxidase	Family
A, B	IPR036460	Copper amine oxidase, catalytic domain superfamily	Homologous Superfamily
A, B	IPR012854	Copper amine oxidase-like, N-terminal	Domain
A, B	IPR015798	Copper amine oxidase, catalytic domain	Domain
A, B	IPR049947	Copper amine oxidase, copper-binding site	Conserved Site
A, B	IPR016182	Copper amine oxidase, N-terminal	Homologous Superfamily
A, B	IPR049948	Copper amine oxidase, TPQ-binding site	Conserved Site
A, B	IPR036582	Copper amine oxidase-like, N-terminal domain superfamily	Homologous Superfamily
A, B	IPR015802	Copper amine oxidase, N3-terminal	Domain
A, B	IPR015800	Copper amine oxidase, N2-terminal	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B	TPQ	Parent Component: TYR RESID: AA0147 PSI-MOD : oxidation of tyrosine to L-2',4',5'-topaquinone MOD:00156

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

Chains	Enzyme Name	Description	Catalytic Residues
A	primary-amine oxidase M-CSA #864	A group of enzymes that oxidise primary monoamines but have little or no activity towards diamines, such as histamine, or towards secondary and tertiary amines. They are copper quinoproteins (2,4,5-trihydroxyphenylalanine quinone) and are sensitive to inhibition by carbonyl-group reagents, such as semicarbazide. In some mammalian tissues the enzyme also functions as a vascular-adhesion protein (VAP-1).	Defined by 6 residues: TYR:A-369ASP:A-383TYR:A-466HIS:A-524HIS:A-526HIS:A-689 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.4.3.6 (PDB Primary Data) Search M-CSA Motif + EC 1.4.3.6 EC: 1.4.3.21 (UniProt) Search M-CSA Motif + EC 1.4.3.21

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.