1CR6

CRYSTAL STRUCTURE OF MURINE SOLUBLE EPOXIDE HYDROLASE COMPLEXED WITH CPU INHIBITOR

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	d1cr6a2	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Epoxide hydrolase	Mammalian epoxide hydrolase, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
A	d1cr6a1	Alpha and beta proteins (a/b)	HAD-like	HAD-like	YihX-like	Epoxide hydrolase, N-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
B	d1cr6b2	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	Epoxide hydrolase	Mammalian epoxide hydrolase, C-terminal domain	house mouse (Mus musculus ) [TaxId: 10090 ],	SCOPe (2.08)
B	d1cr6b1	Alpha and beta proteins (a/b)	HAD-like	HAD-like	YihX-like	Epoxide hydrolase, 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	Epoxide hydrolase	8020157	4000716	SCOP2 (2022-06-29)
A	SCOP2 Family	YihX-like	8025236	4002918	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	alpha/beta-Hydrolases	8032537	3000102	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	HAD-like	8037615	3001890	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	alpha/beta-Hydrolases	8032537	3000102	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	HAD-like	8037615	3001890	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	HAD_2	e1cr6A4	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: HAD_2	ECOD (1.6)
A	Hydrolase_4_2	e1cr6A3	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4_2	ECOD (1.6)
B	HAD_2	e1cr6B1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: HAD-like	F: HAD_2	ECOD (1.6)
B	Hydrolase_4_2	e1cr6B2	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: Hydrolase_4_2	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
B	3.40.50.1000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HAD superfamily/HAD-like	CATH (4.3.0)
B	1.10.150.240	Mainly Alpha	Orthogonal Bundle	DNA polymerase	domain 1	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00561	alpha/beta hydrolase fold (Abhydrolase_1)	alpha/beta hydrolase fold	This catalytic domain is found in a very wide range of enzymes.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	EPOXIDE HYDROLASE	phosphoric ester hydrolase activity hydrolase activity, acting on ester bonds lipid phosphatase activity phosphatase activity hydrolase activity catalytic activity binding toxic substance binding cation binding magnesium ion binding ion binding metal ion binding small molecule binding identical protein binding phosphoric ester hydrolase activity hydrolase activity, acting on ester bonds lipid phosphatase activity phosphatase activity hydrolase activity catalytic activity binding toxic substance binding cation binding magnesium ion binding ion binding metal ion binding small molecule binding identical protein binding protein binding protein homodimerization activity protein dimerization activity lysophosphatidic acid phosphatase activity epoxide hydrolase activity ether hydrolase activity hydrolase activity, acting on ether bonds 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity	stilbene catabolic process catabolic process benzene-containing compound metabolic process olefinic compound catabolic process olefinic compound metabolic process metabolic process cellular process stilbene metabolic process regulation of biosynthetic process regulation of biological process regulation of cellular process biological regulation positive regulation of biological process regulation of macromolecule metabolic process stilbene catabolic process catabolic process benzene-containing compound metabolic process olefinic compound catabolic process olefinic compound metabolic process metabolic process cellular process stilbene metabolic process regulation of biosynthetic process regulation of biological process regulation of cellular process biological regulation positive regulation of biological process regulation of macromolecule metabolic process gene expression macromolecule biosynthetic process positive regulation of macromolecule biosynthetic process regulation of gene expression positive regulation of metabolic process biosynthetic process positive regulation of gene expression positive regulation of biosynthetic process regulation of macromolecule biosynthetic process positive regulation of macromolecule metabolic process macromolecule metabolic process regulation of metabolic process positive regulation of cellular process multicellular organismal process system process circulatory system process regulation of blood pressure positive regulation of blood pressure regulation of biological quality blood circulation sterol homeostasis chemical homeostasis homeostatic process cholesterol homeostasis lipid homeostasis ether metabolic process epoxide metabolic process small molecule metabolic process response to stimulus response to chemical response to toxic substance regulation of cholesterol metabolic process organic hydroxy compound metabolic process sterol metabolic process steroid metabolic process regulation of steroid metabolic process regulation of lipid metabolic process cholesterol metabolic process alcohol metabolic process primary metabolic process regulation of primary metabolic process secondary alcohol metabolic process regulation of small molecule metabolic process lipid metabolic process production of molecular mediator involved in inflammatory response arachidonate metabolite production involved in inflammatory response defense response response to stress prostaglandin production involved in inflammatory response inflammatory response fatty acid metabolic process long-chain fatty acid metabolic process unsaturated fatty acid metabolic process oxoacid metabolic process carboxylic acid metabolic process organic acid metabolic process linoleic acid metabolic process monocarboxylic acid metabolic process dephosphorylation phosphate-containing compound metabolic process phosphorus metabolic process phospholipid dephosphorylation lipid modification	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle organelle peroxisome microbody intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR000639	Epoxide hydrolase-like	Family
A, B	IPR006439	HAD hydrolase, subfamily IA	Family
A, B	IPR023214	HAD superfamily	Homologous Superfamily
A, B	IPR000073	Alpha/beta hydrolase fold-1	Domain
A, B	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
A, B	IPR036412	HAD-like superfamily	Homologous Superfamily
A, B	IPR023198	Phosphoglycolate phosphatase-like, domain 2	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.