Annotations: 3PGB

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	e3pgbA1	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	e3pgbA2	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	DUF1965	e3pgbA3	A: a+b two layers	X: Cystatin-like	H: Amine oxidase N-terminal region (From Topology)	T: Amine oxidase N-terminal region	F: DUF1965	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF09248	Domain of unknown function (DUF1965) (DUF1965)	Domain of unknown function (DUF1965)	Members of this family of fungal domains adopt a structure that consists of an alpha/beta motif. Their exact function has not, as yet, been determined [1].	Domain
A	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	Putative uncharacterized protein	cation binding transition metal ion binding copper ion binding ion binding binding metal ion binding small molecule binding 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 primary methylamine oxidase activity catalytic activity quinone binding	peptidyl-lysine modification primary metabolic process peptidyl-lysine oxidation protein oxidation macromolecule modification peptidyl-amino acid modification metabolic process cellular process protein metabolic process macromolecule metabolic process protein modification process amine metabolic process peptide cross-linking	cell periphery cellular anatomical structure plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000269	Copper amine oxidase	Family
A	IPR015328	Domain of unknown function DUF1965	Domain
A	IPR036460	Copper amine oxidase, catalytic domain superfamily	Homologous Superfamily
A	IPR015798	Copper amine oxidase, catalytic domain	Domain
A	IPR016182	Copper amine oxidase, N-terminal	Homologous Superfamily

Protein Modification Annotation

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

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.