4EV5

Crystal structure of copper amine oxidase-1 from Hansenula polymorpha in complex with benzylamine

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
F	SCOP2B Superfamily	Amine oxidase N-terminal region	8043596	3000455	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Amine oxidase N-terminal region	8043598	3000455	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	amine oxidase catalytic domain	8043593	3001726	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Amine oxidase N-terminal region	8043596	3000455	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Amine oxidase N-terminal region	8043598	3000455	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	amine oxidase catalytic domain	8043593	3001726	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	amine oxidase catalytic domain	8043593	3001726	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Amine oxidase N-terminal region	8043598	3000455	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Amine oxidase N-terminal region	8043596	3000455	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	amine oxidase catalytic domain	8043593	3001726	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Amine oxidase N-terminal region	8043596	3000455	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Amine oxidase N-terminal region	8043598	3000455	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	amine oxidase catalytic domain	8043593	3001726	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Amine oxidase N-terminal region	8043598	3000455	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Amine oxidase N-terminal region	8043596	3000455	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Amine oxidase N-terminal region	8043598	3000455	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	amine oxidase catalytic domain	8043593	3001726	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Amine oxidase N-terminal region	8043596	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)
F	Cu_amine_oxid	e4ev5F8	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Cu_amine_oxid	ECOD (1.6)
F	Cu_amine_oxidN2	e4ev5F9	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)
F	Cu_amine_oxidN3	e4ev5F7	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)
A	Cu_amine_oxid	e4ev5A8	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Cu_amine_oxid	ECOD (1.6)
A	Cu_amine_oxidN2	e4ev5A9	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	e4ev5A7	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	e4ev5B8	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Cu_amine_oxid	ECOD (1.6)
B	Cu_amine_oxidN2	e4ev5B9	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	e4ev5B7	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)
C	Cu_amine_oxid	e4ev5C8	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Cu_amine_oxid	ECOD (1.6)
C	Cu_amine_oxidN2	e4ev5C9	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)
C	Cu_amine_oxidN3	e4ev5C7	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)
D	Cu_amine_oxid	e4ev5D8	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Cu_amine_oxid	ECOD (1.6)
D	Cu_amine_oxidN2	e4ev5D9	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)
D	Cu_amine_oxidN3	e4ev5D7	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)
E	Cu_amine_oxid	e4ev5E8	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Cu_amine_oxid	ECOD (1.6)
E	Cu_amine_oxidN2	e4ev5E9	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)
E	Cu_amine_oxidN3	e4ev5E7	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)
F	3.10.450.40	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
F	2.70.98.20	Mainly Beta	Distorted Sandwich	Beta-galactosidase	Chain A, domain 5	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	3.10.450.40	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)
C	3.10.450.40	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
C	2.70.98.20	Mainly Beta	Distorted Sandwich	Beta-galactosidase	Chain A, domain 5	CATH (4.3.0)
D	3.10.450.40	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
D	2.70.98.20	Mainly Beta	Distorted Sandwich	Beta-galactosidase	Chain A, domain 5	CATH (4.3.0)
E	3.10.450.40	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
E	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, C, D, E A, B, C, D, E, F	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, C, D, E A, B, C, D, E, F	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, C, D, E A, B, C, D, E, F	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, C, D, E A, B, C, D, E, F	Peroxisomal primary 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 binding quinone binding small molecule binding cation binding transition metal ion binding copper ion binding ion binding 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 binding quinone binding small molecule binding cation binding transition metal ion binding copper ion binding ion binding metal ion binding primary methylamine oxidase activity	amine metabolic process metabolic process cellular process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure organelle peroxisome microbody cytoplasm intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

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

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.