Annotations: 3K4C

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	F_UNCLASSIFIED	e3k4cA1	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: F_UNCLASSIFIED	ECOD (1.6)
A	PF05199	e3k4cA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF05199	ECOD (1.6)
B	F_UNCLASSIFIED	e3k4cB1	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: F_UNCLASSIFIED	ECOD (1.6)
B	PF05199	e3k4cB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF05199	ECOD (1.6)
C	F_UNCLASSIFIED	e3k4cC1	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: F_UNCLASSIFIED	ECOD (1.6)
C	PF05199	e3k4cC2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF05199	ECOD (1.6)
D	F_UNCLASSIFIED	e3k4cD1	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: F_UNCLASSIFIED	ECOD (1.6)
D	PF05199	e3k4cD2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF05199	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1920.50	Alpha Beta	2-Layer Sandwich	Phage tail proteins - 2 layer sandwich fold		CATH (4.3.0)
B	3.30.1920.50	Alpha Beta	2-Layer Sandwich	Phage tail proteins - 2 layer sandwich fold		CATH (4.3.0)
C	3.30.1920.50	Alpha Beta	2-Layer Sandwich	Phage tail proteins - 2 layer sandwich fold		CATH (4.3.0)
D	3.30.1920.50	Alpha Beta	2-Layer Sandwich	Phage tail proteins - 2 layer sandwich fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF05199	GMC oxidoreductase (GMC_oxred_C)	GMC oxidoreductase	This domain found associated with Pfam:PF00732.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Pyranose 2-oxidase	oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen catalytic activity oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor oxidoreductase activity, acting on CH-OH group of donors pyranose oxidase activity flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding oxidoreductase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen catalytic activity oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor oxidoreductase activity, acting on CH-OH group of donors pyranose oxidase activity flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding	-	periplasmic space cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR012814	Pyranose 2-oxidase	Family
A, B, C, D	IPR007867	Glucose-methanol-choline oxidoreductase, C-terminal	Domain
A, B, C, D	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily

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 R01GM133198.