4OMC

X-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-Amba

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d4omca2	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d4omca1	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d4omcb2	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d4omcb1	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d4omcc2	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d4omcc1	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d4omcd2	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d4omcd1	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d4omce2	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d4omce1	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d4omcf2	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d4omcf1	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF01483	e4omcA2	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF01483	ECOD (1.6)
A	PF00082	e4omcA1	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: PF00082	ECOD (1.6)
B	PF01483	e4omcB2	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF01483	ECOD (1.6)
B	PF00082	e4omcB1	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: PF00082	ECOD (1.6)
C	PF01483	e4omcC2	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF01483	ECOD (1.6)
C	PF00082	e4omcC1	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: PF00082	ECOD (1.6)
D	PF01483	e4omcD2	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF01483	ECOD (1.6)
D	PF00082	e4omcD1	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: PF00082	ECOD (1.6)
E	PF01483	e4omcE2	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF01483	ECOD (1.6)
E	PF00082	e4omcE1	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: PF00082	ECOD (1.6)
F	PF01483	e4omcF2	A: beta sandwiches	X: jelly-roll	H: Galactose-binding domain-like (From Topology)	T: Galactose-binding domain-like	F: PF01483	ECOD (1.6)
F	PF00082	e4omcF1	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: PF00082	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.200	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Peptidase S8/S53 domain	CATH (4.3.0)
A	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
B	3.40.50.200	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Peptidase S8/S53 domain	CATH (4.3.0)
B	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
C	3.40.50.200	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Peptidase S8/S53 domain	CATH (4.3.0)
C	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
D	3.40.50.200	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Peptidase S8/S53 domain	CATH (4.3.0)
D	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
E	3.40.50.200	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Peptidase S8/S53 domain	CATH (4.3.0)
E	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
F	3.40.50.200	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Peptidase S8/S53 domain	CATH (4.3.0)
F	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	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	PF00082	Subtilase family (Peptidase_S8)	Subtilase family	Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see Pfam:PF00089). Structure is an alpha/beta fold containing a 7 ...	Subtilases are a family of serine proteases. They appear to have independently and convergently evolved an Asp/Ser/His catalytic triad, like that found in the trypsin serine proteases (see Pfam:PF00089). Structure is an alpha/beta fold containing a 7-stranded parallel beta sheet, order 2314567.	Domain
A, B, C, D, E A, B, C, D, E, F	PF01483	Proprotein convertase P-domain (P_proprotein)	Proprotein convertase P-domain	-	Family

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	Furin	neurotrophin binding protein binding binding nerve growth factor binding growth factor binding peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity cation binding neurotrophin binding protein binding binding nerve growth factor binding growth factor binding peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity cation binding ion binding metal ion binding small molecule binding enzyme binding protease binding glycosaminoglycan binding organic acid binding heparan sulfate binding anion binding carboxylic acid binding carbohydrate derivative binding sulfur compound binding enzyme regulator activity molecular function inhibitor activity peptidase regulator activity serine-type endopeptidase inhibitor activity molecular function regulator activity enzyme inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity peptide binding heparin binding	organic substance metabolic process peptide biosynthetic process biosynthetic process organic substance biosynthetic process metabolic process peptide metabolic process viral process viral life cycle organonitrogen compound catabolic process regulation of biological process organonitrogen compound metabolic process catabolic process regulation of protein metabolic process biological regulation organic substance metabolic process peptide biosynthetic process biosynthetic process organic substance biosynthetic process metabolic process peptide metabolic process viral process viral life cycle organonitrogen compound catabolic process regulation of biological process organonitrogen compound metabolic process catabolic process regulation of protein metabolic process biological regulation primary metabolic process regulation of macromolecule metabolic process protein catabolic process regulation of catabolic process macromolecule catabolic process regulation of primary metabolic process protein metabolic process macromolecule metabolic process regulation of metabolic process organic substance catabolic process regulation of protein catabolic process nerve growth factor production multicellular organismal process neurotrophin production cellular component organization extracellular matrix organization cellular process cellular component organization or biogenesis extracellular structure organization external encapsulating structure organization cellular biosynthetic process cellular metabolic process signal peptide processing gene expression macromolecule biosynthetic process protein maturation proteolysis protein processing cytokine precursor processing signaling receptor ligand precursor processing cytokine production viral gene expression viral protein processing viral translation regulation of defense response response to stimulus regulation of response to external stimulus negative regulation of inflammatory response negative regulation of biological process inflammatory response to antigenic stimulus response to stress regulation of response to stress regulation of immune system process negative regulation of inflammatory response to antigenic stimulus defense response immune response negative regulation of response to stimulus negative regulation of immune response regulation of inflammatory response to antigenic stimulus response to external stimulus regulation of inflammatory response regulation of response to stimulus negative regulation of immune system process immune system process negative regulation of response to external stimulus negative regulation of defense response regulation of immune response inflammatory response biological process involved in interspecies interaction between organisms positive regulation of viral life cycle positive regulation of viral process positive regulation of biological process modulation by symbiont of entry into host biological process involved in interaction with host biological process involved in symbiotic interaction regulation of viral entry into host cell regulation of viral life cycle regulation of viral process symbiont entry into host cell symbiont entry into host positive regulation of viral entry into host cell positive regulation by symbiont of entry into host regulation of biological process involved in symbiotic interaction regulation of cellular process positive regulation of protein metabolic process positive regulation of membrane protein ectodomain proteolysis positive regulation of cellular metabolic process cellular catabolic process positive regulation of metabolic process regulation of proteolysis membrane protein proteolysis positive regulation of macromolecule metabolic process positive regulation of cellular process membrane protein ectodomain proteolysis regulation of membrane protein ectodomain proteolysis regulation of cellular metabolic process positive regulation of protein catabolic process positive regulation of catabolic process positive regulation of proteolysis regulation of cellular catabolic process positive regulation of cellular catabolic process regulation of catalytic activity regulation of peptidase activity regulation of molecular function regulation of hydrolase activity regulation of endopeptidase activity cellular response to stimulus cellular response to growth factor stimulus cell surface receptor protein serine/threonine kinase signaling pathway cell surface receptor signaling pathway signaling cellular response to transforming growth factor beta stimulus response to endogenous stimulus cell communication cellular response to endogenous stimulus response to transforming growth factor beta transforming growth factor beta receptor signaling pathway response to growth factor transforming growth factor beta receptor superfamily signaling pathway signal transduction enzyme-linked receptor protein signaling pathway developmental process chordate embryonic development embryo development in utero embryonic development multicellular organism development anatomical structure morphogenesis blastocyst formation embryo development ending in birth or egg hatching anatomical structure development anatomical structure formation involved in morphogenesis blastocyst development collagen catabolic process collagen metabolic process negative regulation of cellular catabolic process receptor catabolic process negative regulation of cellular metabolic process negative regulation of protein catabolic process negative regulation of low-density lipoprotein particle receptor catabolic process receptor metabolic process negative regulation of cellular process regulation of low-density lipoprotein particle receptor catabolic process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process negative regulation of catabolic process negative regulation of receptor catabolic process negative regulation of metabolic process low-density lipoprotein particle receptor catabolic process low-density lipoprotein receptor particle metabolic process regulation of receptor catabolic process regulation of signaling regulation of signal transduction regulation of cell communication amyloid fibril formation supramolecular fiber organization plasma lipoprotein particle organization protein-containing complex organization protein-containing complex remodeling protein-lipid complex organization plasma lipoprotein particle remodeling regulation of plasma lipoprotein particle levels protein-lipid complex remodeling peptide hormone processing amide metabolic process regulation of biological quality regulation of hormone levels hormone metabolic process cellular component disassembly extracellular matrix disassembly regulation of transforming growth factor beta production transforming growth factor beta1 production regulation of transforming growth factor beta1 production regulation of cytokine production regulation of multicellular organismal process transforming growth factor beta production regulation of biosynthetic process negative regulation of transforming growth factor beta1 production negative regulation of cytokine production negative regulation of cellular biosynthetic process negative regulation of transforming growth factor beta production regulation of cellular biosynthetic process regulation of gene expression negative regulation of gene expression negative regulation of biosynthetic process negative regulation of macromolecule biosynthetic process regulation of macromolecule biosynthetic process negative regulation of multicellular organismal process dibasic protein processing localization secretion by cell secretion transport export from cell establishment of localization regulation of sterol transport regulation of localization regulation of transport organic substance transport lipid localization lipid transport regulation of lipid transport organic hydroxy compound transport regulation of lipid localization macromolecule localization cholesterol transport sterol transport regulation of cholesterol transport zymogen activation	membrane cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure Golgi apparatus subcompartment Golgi apparatus membrane cellular anatomical entity extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space vesicle extracellular membrane-bounded organelle intracellular anatomical structure Golgi apparatus subcompartment Golgi apparatus organelle subcompartment intracellular membrane-bounded organelle endomembrane system intracellular organelle trans-Golgi network cytoplasm Golgi membrane bounding membrane of organelle organelle membrane endosome membrane endosome intracellular vesicle cytoplasmic vesicle membrane vesicle membrane cytoplasmic vesicle cell surface cell periphery plasma membrane membrane microdomain membrane raft membrane-enclosed lumen intracellular organelle lumen Golgi lumen organelle lumen transport vesicle trans-Golgi network transport vesicle clathrin-coated vesicle coated vesicle Golgi-associated vesicle endoplasmic reticulum
G [auth H], H [auth I], I [auth J], J [auth K], K [auth L], G [auth H], H [auth I], I [auth J], J [auth K], K [auth L], L [auth N]	meta-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)benzamidine	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR032815	Peptidase S8, pro-domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR034182	Kexin/furin catalytic domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR002884	P domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR023828	Peptidase S8, subtilisin, Ser-active site	Active Site
A, B, C, D, E A, B, C, D, E, F	IPR022398	Peptidase S8, subtilisin, His-active site	Active Site
A, B, C, D, E A, B, C, D, E, F	IPR000209	Peptidase S8/S53 domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR015500	Peptidase S8, subtilisin-related	Family
A, B, C, D, E A, B, C, D, E, F	IPR006212	Furin-like repeat	Repeat
A, B, C, D, E A, B, C, D, E, F	IPR008979	Galactose-binding-like domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR023827	Peptidase S8, subtilisin, Asp-active site	Active Site
A, B, C, D, E A, B, C, D, E, F	IPR036852	Peptidase S8/S53 domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR009030	Growth factor receptor cysteine-rich domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR038466	Peptidase S8, pro-domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F	Pharos: P09958	carcinoma sarcomatoid carcinoma Mammary Neoplasms, Experimental psoriasis undifferentiated carcinoma autism spectrum disorder endogenous depression influenza mammary neoplasms, animal myocardial infarction bipolar disorder heart disease lung carcinoma pancreatic ductal adenocarcinoma severe acute respiratory syndrome carcinoma sarcomatoid carcinoma Mammary Neoplasms, Experimental psoriasis undifferentiated carcinoma autism spectrum disorder endogenous depression influenza mammary neoplasms, animal myocardial infarction bipolar disorder heart disease lung carcinoma pancreatic ductal adenocarcinoma severe acute respiratory syndrome attention deficit hyperactivity disorder, inattentive type breast carcinoma COVID-19 hypertensive disorder Middle East respiratory syndrome

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.