1EIN

THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE

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
Membrane Protein Annotation: OPM

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1eina_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Fungal lipases	Triacylglycerol lipase	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
B	d1einb_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Fungal lipases	Triacylglycerol lipase	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)
C	d1einc_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Fungal lipases	Triacylglycerol lipase	(Thermomyces lanuginosus ) [TaxId: 5541 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	alpha/beta-Hydrolases	8032578	3000102	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	alpha/beta-Hydrolases	8032578	3000102	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	alpha/beta-Hydrolases	8032578	3000102	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	Lipase_3	e1einA1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Lipase_3	ECOD (1.6)
B	Lipase_3	e1einB1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Lipase_3	ECOD (1.6)
C	Lipase_3	e1einC1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Lipase_3	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
B	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
C	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF03893	Lipase 3 N-terminal region (Lipase3_N)	Lipase 3 N-terminal region	N terminal region to Pfam:PF01764, found on a subset of Lipase 3 containing proteins.	Domain
A, B, C	PF01764	Lipase (class 3) (Lipase_3)	Lipase (class 3)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	LIPASE	triacylglycerol lipase activity hydrolase activity, acting on ester bonds carboxylic ester hydrolase activity hydrolase activity catalytic activity lipase activity	lipid catabolic process catabolic process metabolic process primary metabolic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR002921	Fungal lipase-type domain	Domain
A, B, C	IPR005592	Mono-/di-acylglycerol lipase, N-terminal	Domain
A, B, C	IPR051299	Alpha/beta hydrolase lipase/esterase	Family
A, B, C	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B, C	OPM	Monotopic/peripheral	Alpha/Beta monotopic/peripheral	Alpha/beta-hydrolases	Fungal lipases

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.