6WV5

Human VKOR C43S mutant with vitamin K1 epoxide

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations
Membrane Protein Annotation: OPM
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD
Membrane Protein Annotation: mpstruc

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	GFP-like	8106992	3000576	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	GFP-like	8096046	3000576	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	GFP	e6wv5A1	A: beta barrels	X: GFP-like (From Topology)	H: GFP-like (From Topology)	T: GFP-like	F: GFP	ECOD (1.6)
A	VKOR	e6wv5A2	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)

Protein Family Annotation Pfam Database Homepage

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
A	PF01353	Green fluorescent protein (GFP)	Green fluorescent protein	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Vitamin K epoxide reductase Cys43Ser mutant, termini restrained by green fluorescent protein	oxidoreductase activity oxidoreductase activity, acting on CH or CH2 groups oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor vitamin-K-epoxide reductase (warfarin-sensitive) activity catalytic activity binding quinone binding small molecule binding vitamin-K-epoxide reductase (warfarin-insensitive) activity	multicellular organismal process regulation of body fluid levels wound healing response to stimulus hemostasis biological regulation blood coagulation response to stress coagulation regulation of biological quality response to wounding peptidyl-glutamic acid modification macromolecule modification peptidyl-amino acid modification multicellular organismal process regulation of body fluid levels wound healing response to stimulus hemostasis biological regulation blood coagulation response to stress coagulation regulation of biological quality response to wounding peptidyl-glutamic acid modification macromolecule modification peptidyl-amino acid modification peptidyl-glutamic acid carboxylation metabolic process primary metabolic process protein metabolic process macromolecule metabolic process protein carboxylation protein modification process positive regulation of coagulation regulation of biological process positive regulation of biological process positive regulation of multicellular organismal process regulation of multicellular organismal process regulation of coagulation cellular response to stimulus cellular response to chemical stimulus response to chemical cellular response to xenobiotic stimulus cellular metabolic process cellular process xenobiotic metabolic process response to xenobiotic stimulus developmental process multicellular organism development skeletal system development anatomical structure development animal organ development bone development system development regulation of response to external stimulus regulation of blood coagulation response to external stimulus regulation of response to wounding regulation of response to stimulus regulation of response to stress regulation of wound healing regulation of hemostasis response to organic cyclic compound vitamin K metabolic process cellular ketone metabolic process fat-soluble vitamin metabolic process small molecule metabolic process vitamin metabolic process bioluminescence generation of precursor metabolites and energy	membrane-bounded organelle intracellular organelle intracellular anatomical structure organelle endoplasmic reticulum cytoplasm cellular anatomical entity intracellular membrane-bounded organelle endomembrane system organelle subcompartment membrane endoplasmic reticulum subcompartment nuclear outer membrane-endoplasmic reticulum membrane network organelle membrane membrane-bounded organelle intracellular organelle intracellular anatomical structure organelle endoplasmic reticulum cytoplasm cellular anatomical entity intracellular membrane-bounded organelle endomembrane system organelle subcompartment membrane endoplasmic reticulum subcompartment nuclear outer membrane-endoplasmic reticulum membrane network organelle membrane endoplasmic reticulum membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR042406	Vitamin K epoxide reductase complex subunit 1	Family
A	IPR038354	VKOR domain superfamily	Homologous Superfamily
A	IPR012932	Vitamin K epoxide reductase	Domain
A	IPR000786	Green fluorescent protein, GFP	Family
A	IPR011584	Green fluorescent protein-related	Family
A	IPR009017	Green fluorescent protein	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: Q9BQB6	coumarin resistance vitamin K-dependent clotting factors, combined deficiency of, type 2 Warfarin resistance psoriasis vitamin K-dependent clotting factors, combined deficiency of, type 1 aortic aneurysm vascular disease Hashimoto thyroiditis lung cancer myocardial infarction ovarian cancer pancreatic intraductal papillary-mucinous neoplasm plasma cell myeloma blood coagulation disease cerebrovascular disorder coumarin resistance vitamin K-dependent clotting factors, combined deficiency of, type 2 Warfarin resistance psoriasis vitamin K-dependent clotting factors, combined deficiency of, type 1 aortic aneurysm vascular disease Hashimoto thyroiditis lung cancer myocardial infarction ovarian cancer pancreatic intraductal papillary-mucinous neoplasm plasma cell myeloma blood coagulation disease cerebrovascular disorder glioblastoma malignant glioma pancreatic ductal adenocarcinoma pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia atrial fibrillation coronary artery disease thrombotic disease Graves disease intracranial embolism medulloblastoma osteosarcoma pancreatic intraductal papillary-mucinous carcinoma pilocytic astrocytoma atypical teratoid rhabdoid tumor pulmonary embolism

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A	OPM				Vitamin K epoxide reductase

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A	MemProtMD	Annotated as membrane protein by MemProtMD

Membrane Protein Annotation: mpstruc mpstruc Database Homepage

Chains	Resource Link	Group	Subgroup	Protein
A	mpstruc	TRANSMEMBRANE PROTEINS: ALPHA-HELICAL	Oxidoreductases	Vitamin K epoxide reductase (VKOR) with warfarin

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.