4NV6

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	VKOR	e4nv6A2	A: alpha bundles	X: Bromodomain-like	H: Vitamin K epoxide reductase (VKOR) (From Topology)	T: Vitamin K epoxide reductase (VKOR)	F: VKOR	ECOD (1.6)
A	DSBA_1	e4nv6A1	A: a+b three layers	X: Thioredoxin-like	H: Thioredoxin-like (From Topology)	T: Thioredoxin-like	F: DSBA_1	ECOD (1.6)

Chains	Accession	Name	Description	Comments	Source
A	PF07884	Vitamin K epoxide reductase family (VKOR)	Vitamin K epoxide reductase family	Vitamin K epoxide reductase (VKOR) recycles reduced vitamin K, which is used subsequently as a co-factor in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. VKORC1 is a member of a large family of predicted enzymes that ...	Vitamin K epoxide reductase (VKOR) recycles reduced vitamin K, which is used subsequently as a co-factor in the gamma-carboxylation of glutamic acid residues in blood coagulation enzymes. VKORC1 is a member of a large family of predicted enzymes that are present in vertebrates, Drosophila, plants, bacteria and archaea [1]. Four cysteine residues and one residue, which is either serine or threonine, are identified as likely active-site residues [1]. In some plant and bacterial homologues the VKORC1 homologous domain is fused with domains of the thioredoxin family of oxidoreductases [1].	Domain

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	VKORC1/thioredoxin domain protein	oxidoreductase activity catalytic activity binding quinone binding small molecule binding	-	cellular anatomical structure membrane

Chains	Accession	Name	Type
A	IPR038354	VKOR domain superfamily	Homologous Superfamily
A	IPR012932	Vitamin K epoxide reductase	Domain
A	IPR036249	Thioredoxin-like superfamily	Homologous Superfamily
A	IPR044698	Vitamin K epoxide reductase-like VKOR/LOT1	Domain