Annotations: 1FLE

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth E]	d1flee_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Elastase	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
B [auth I]	d1flei_	Small proteins	Knottins (small inhibitors, toxins, lectins)	Elafin-like	Elafin-like	Elafin, elastase-specific inhibitor	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth E]	SCOP2B Superfamily	Trypsin-like serine proteases	8039111	3000114	SCOP2B (2022-06-29)
B [auth I]	SCOP2 Family	Elafin-like	8025993	4003241	SCOP2 (2022-06-29)
B [auth I]	SCOP2 Superfamily	Elafin-like	8038372	3000478	SCOP2 (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 [auth E]	Trypsin_1	e1fleE1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
B [auth I]	WAP	e1fleI1	A: few secondary structure elements	X: Elafin-like (From Topology)	H: Elafin-like (From Topology)	T: Elafin-like	F: WAP	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth E]	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
B [auth I]	4.10.75.10	Few Secondary Structures	Irregular	R-elafin	Elafin-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth E]	PF00089	Trypsin (Trypsin)	Trypsin		Domain
B [auth I]	PF00095	WAP-type (Whey Acidic Protein) 'four-disulfide core' (WAP)	WAP-type (Whey Acidic Protein) 'four-disulfide core'	WAP belongs to the group of Elafin or elastase-specific inhibitors.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth E]	ELASTASE	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 binding metal ion binding small molecule binding	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process	cellular anatomical structure extracellular region extracellular space
B [auth I]	ELAFIN	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 structural constituent of skin epidermis structural molecule activity	behavior multicellular organismal process reproductive process multicellular organismal reproductive process reproductive behavior mating behavior copulation humoral immune response biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response immune response antibacterial humoral response behavior multicellular organismal process reproductive process multicellular organismal reproductive process reproductive behavior mating behavior copulation humoral immune response biological process involved in interspecies interaction between organisms response to stimulus response to other organism defense response immune response antibacterial humoral response defense response to symbiont response to external stimulus antimicrobial humoral response response to biotic stimulus defense response to bacterium defense response to other organism response to stress immune system process response to bacterium response to external biotic stimulus innate immune response peptide cross-linking macromolecule modification metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process protein modification process	cell periphery cellular anatomical structure plasma membrane membrane cornified envelope extracellular region intracellular anatomical structure cytoplasm cytosol extracellular matrix external encapsulating structure extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth E]	IPR001254	Serine proteases, trypsin domain	Domain
A [auth E]	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A [auth E]	IPR050850	Peptidase S1 family, Elastase subfamily	Family
A [auth E]	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
A [auth E]	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
A [auth E]	IPR001314	Peptidase S1A, chymotrypsin family	Family
A [auth E]	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
B [auth I]	IPR036645	Elafin-like superfamily	Homologous Superfamily
B [auth I]	IPR002098	Seminal vesicle protein I	Repeat
B [auth I]	IPR050514	WAP four-disulfide core domain	Family
B [auth I]	IPR019541	Trappin protein transglutaminase-binding repeat	Repeat
B [auth I]	IPR008197	WAP-type 'four-disulfide core' domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
B [auth I]	Pharos: P19957	contact dermatitis bipolar disorder psoriasis Contact hypersensitivity

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A [auth E], B [auth I]	OPM				Elafin-like

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.