1P8J

CRYSTAL STRUCTURE OF THE PROPROTEIN CONVERTASE FURIN

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1p8ja1	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	Proprotein convertase P-domain	Furin, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
A	d1p8ja2	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	Furin, N-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
B	d1p8jb1	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	Proprotein convertase P-domain	Furin, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
B	d1p8jb2	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	Furin, N-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
C	d1p8jc1	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	Proprotein convertase P-domain	Furin, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
C	d1p8jc2	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	Furin, N-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
D	d1p8jd1	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	Proprotein convertase P-domain	Furin, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
D	d1p8jd2	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	Furin, N-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
F	d1p8jf1	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	Proprotein convertase P-domain	Furin, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
F	d1p8jf2	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	Furin, N-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
G	d1p8jg1	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	Proprotein convertase P-domain	Furin, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
G	d1p8jg2	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	Furin, N-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
H	d1p8jh1	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	Proprotein convertase P-domain	Furin, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
H	d1p8jh2	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	Furin, N-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
E	d1p8je1	All beta proteins	Galactose-binding domain-like	Galactose-binding domain-like	Proprotein convertase P-domain	Furin, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
E	d1p8je2	Alpha and beta proteins (a/b)	Subtilisin-like	Subtilisin-like	Subtilases	Furin, N-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	proprotein convertase p-domain	8022300	4003911	SCOP2 (2022-06-29)
A	SCOP2 Family	Subtilases	8022301	4000409	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	galactose-binding domain-like	8034680	3000087	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Subtilisin-like	8034681	3000226	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	galactose-binding domain-like	8034680	3000087	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Subtilisin-like	8034681	3000226	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	galactose-binding domain-like	8034680	3000087	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Subtilisin-like	8034681	3000226	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	galactose-binding domain-like	8034680	3000087	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Subtilisin-like	8034681	3000226	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Subtilisin-like	8034681	3000226	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	galactose-binding domain-like	8034680	3000087	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Subtilisin-like	8034681	3000226	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	galactose-binding domain-like	8034680	3000087	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	galactose-binding domain-like	8034680	3000087	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Subtilisin-like	8034681	3000226	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Subtilisin-like	8034681	3000226	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	galactose-binding domain-like	8034680	3000087	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	P_proprotein	e1p8jA1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: P_proprotein	ECOD (1.6)
A	Peptidase_S8	e1p8jA2	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: Peptidase_S8	ECOD (1.6)
B	P_proprotein	e1p8jB1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: P_proprotein	ECOD (1.6)
B	Peptidase_S8	e1p8jB2	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: Peptidase_S8	ECOD (1.6)
C	P_proprotein	e1p8jC1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: P_proprotein	ECOD (1.6)
C	Peptidase_S8	e1p8jC2	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: Peptidase_S8	ECOD (1.6)
D	P_proprotein	e1p8jD1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: P_proprotein	ECOD (1.6)
D	Peptidase_S8	e1p8jD2	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: Peptidase_S8	ECOD (1.6)
F	P_proprotein	e1p8jF1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: P_proprotein	ECOD (1.6)
F	Peptidase_S8	e1p8jF2	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: Peptidase_S8	ECOD (1.6)
G	P_proprotein	e1p8jG1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: P_proprotein	ECOD (1.6)
G	Peptidase_S8	e1p8jG2	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: Peptidase_S8	ECOD (1.6)
H	P_proprotein	e1p8jH1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: P_proprotein	ECOD (1.6)
H	Peptidase_S8	e1p8jH2	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: Peptidase_S8	ECOD (1.6)
E	P_proprotein	e1p8jE1	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: P_proprotein	ECOD (1.6)
E	Peptidase_S8	e1p8jE2	A: a/b three-layered sandwiches	X: Subtilisin-like	H: Subtilisin-like (From Topology)	T: Subtilisin-like	F: Peptidase_S8	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)
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)
G	3.40.50.200	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Peptidase S8/S53 domain	CATH (4.3.0)
G	2.60.120.260	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding domain-like	CATH (4.3.0)
H	3.40.50.200	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Peptidase S8/S53 domain	CATH (4.3.0)
H	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	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, G, H	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, G, H	Furin precursor	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	peptide biosynthetic process biosynthetic process metabolic process cellular process peptide metabolic process viral process viral life cycle nerve growth factor production multicellular organismal process neurotrophin production signal peptide processing primary metabolic process gene expression macromolecule biosynthetic process peptide biosynthetic process biosynthetic process metabolic process cellular process peptide metabolic process viral process viral life cycle nerve growth factor production multicellular organismal process neurotrophin production signal peptide processing primary metabolic process gene expression macromolecule biosynthetic process protein maturation proteolysis protein processing protein metabolic process macromolecule metabolic process cytokine precursor processing signaling receptor ligand precursor processing cytokine production regulation of biological process biological process involved in interspecies interaction between organisms positive regulation of viral life cycle positive regulation of viral process biological regulation 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 regulation of catalytic activity regulation of protein metabolic process regulation of peptidase activity regulation of macromolecule metabolic process regulation of primary metabolic process regulation of molecular function regulation of proteolysis regulation of hydrolase activity regulation of endopeptidase activity regulation of metabolic process 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 receptor catabolic process catabolic process negative regulation of biological process macromolecule catabolic process negative regulation of protein catabolic process cellular 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 protein catabolic process regulation of catabolic process low-density lipoprotein receptor particle metabolic process regulation of receptor catabolic process regulation of protein catabolic process cellular response to stimulus regulation of signaling response to stimulus signaling regulation of signal transduction cell communication regulation of response to stimulus regulation of cell communication signal transduction peptide hormone processing regulation of hormone levels hormone metabolic process amide metabolic process regulation of biological quality 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 transforming growth factor beta production 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 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	cellular anatomical structure membrane membrane-bounded organelle intracellular anatomical structure Golgi apparatus subcompartment Golgi apparatus organelle subcompartment intracellular membrane-bounded organelle endomembrane system intracellular organelle organelle trans-Golgi network cytoplasm membrane-enclosed lumen cellular anatomical structure membrane membrane-bounded organelle intracellular anatomical structure Golgi apparatus subcompartment Golgi apparatus organelle subcompartment intracellular membrane-bounded organelle endomembrane system intracellular organelle organelle trans-Golgi network cytoplasm membrane-enclosed lumen intracellular organelle lumen endoplasmic reticulum lumen organelle lumen endoplasmic reticulum Golgi membrane bounding membrane of organelle organelle membrane endosome membrane endosome intracellular vesicle cytoplasmic vesicle membrane vesicle membrane cytoplasmic vesicle vesicle cell surface cell periphery plasma membrane membrane microdomain membrane raft transport vesicle membrane trans-Golgi network transport vesicle membrane trans-Golgi network transport vesicle clathrin-coated vesicle coated vesicle Golgi-associated vesicle clathrin-coated vesicle membrane transport vesicle coated vesicle membrane Golgi-associated vesicle membrane early endosome extracellular region
I [auth J], J [auth K], K [auth L], L [auth M], M [auth N], I [auth J], J [auth K], K [auth L], L [auth M], M [auth N], N [auth P], O [auth Q], P [auth R]	DECANOYL-ARG-VAL-LYS-ARG-CHLOROMETHYLKETONE INHIBITOR	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR032815	Peptidase S8, pro-domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR034182	Kexin/furin catalytic domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR002884	P domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR023828	Peptidase S8, subtilisin, Ser-active site	Active Site
A, B, C, D, E A, B, C, D, E, F, G, H	IPR022398	Peptidase S8, subtilisin, His-active site	Active Site
A, B, C, D, E A, B, C, D, E, F, G, H	IPR000209	Peptidase S8/S53 domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR015500	Peptidase S8, subtilisin-related	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR006212	Furin-like repeat	Repeat
A, B, C, D, E A, B, C, D, E, F, G, H	IPR008979	Galactose-binding-like domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR023827	Peptidase S8, subtilisin, Asp-active site	Active Site
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036852	Peptidase S8/S53 domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR009030	Growth factor receptor cysteine-rich domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR038466	Peptidase S8, pro-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 R01GM157729.