6AP7

Crystal Structure of DAD2 in complex with 2-(2-methyl-3-nitroanilino)benzoic acid

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d6ap7b_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	automated matches	automated matches	Petunia (Petunia x hybrida ) [TaxId: 4102 ],	SCOPe (2.08)
A	d6ap7a_	Alpha and beta proteins (a/b)	alpha/beta-Hydrolases	alpha/beta-Hydrolases	automated matches	automated matches	Petunia (Petunia x hybrida ) [TaxId: 4102 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	Hydrolase_4_1	e6ap7B1	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_1	ECOD (1.6)
A	Hydrolase_4_1	e6ap7A1	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_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

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

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF12697	Alpha/beta hydrolase family (Abhydrolase_6)	Alpha/beta hydrolase family	This family contains alpha/beta hydrolase enzymes of diverse specificity.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Probable strigolactone esterase DAD2	hydrolase activity, acting on ester bonds hydrolase activity catalytic activity	developmental process multicellular organismal process shoot system morphogenesis shoot axis formation anatomical structure morphogenesis multicellular organism development morphogenesis of a branching structure secondary shoot formation anatomical structure development anatomical structure formation involved in morphogenesis shoot system development plant organ formation system development isoprenoid biosynthetic process developmental process multicellular organismal process shoot system morphogenesis shoot axis formation anatomical structure morphogenesis multicellular organism development morphogenesis of a branching structure secondary shoot formation anatomical structure development anatomical structure formation involved in morphogenesis shoot system development plant organ formation system development isoprenoid biosynthetic process cellular biosynthetic process cellular metabolic process strigolactone biosynthetic process sesquiterpenoid metabolic process lipid biosynthetic process primary metabolic process terpenoid biosynthetic process biosynthetic process lactone biosynthetic process lactone metabolic process cellular lipid metabolic process metabolic process cellular process sesquiterpenoid biosynthetic process strigolactone metabolic process terpenoid metabolic process isoprenoid metabolic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR000073	Alpha/beta hydrolase fold-1	Domain
A, B	IPR029058	Alpha/Beta hydrolase fold	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.