Annotations: 5IL5

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF14765	e5il5A1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF14765	ECOD (1.6)
A	PF21089	e5il5A2	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF21089	ECOD (1.6)
B	PF14765	e5il5B2	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF14765	ECOD (1.6)
B	PF21089	e5il5B1	A: a+b two layers	X: Thioesterase/thiol ester dehydrase-isomerase-like	H: Thioesterase/thiol ester dehydrase-isomerase (From Topology)	T: Thioesterase/thiol ester dehydrase-isomerase	F: PF21089	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF21089	Polyketide synthase dehydratase domain (PKS_DH_N)	Polyketide synthase dehydratase domain	This domain is part of a dehydratase domain found in diverse PKS enzymes. This domain adopts a HotDog fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	MlnD	vitamin binding amide binding modified amino acid binding binding phosphopantetheine binding small molecule binding acyltransferase activity 3-oxoacyl-[acyl-carrier-protein] synthase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity	fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process biosynthetic process fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process biosynthetic process organic substance biosynthetic process cellular lipid metabolic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR014031	Beta-ketoacyl synthase, C-terminal	Domain
A, B	IPR006162	Phosphopantetheine attachment site	PTM
A, B	IPR049490	C883_1060-like, ketoreductase domain, N-terminal	Domain
A, B	IPR032821	Polyketide synthase, C-terminal extension	Domain
A, B	IPR009081	Phosphopantetheine binding ACP domain	Domain
A, B	IPR014030	Beta-ketoacyl synthase, N-terminal	Domain
A, B	IPR049552	Polyketide synthase, dehydratase domain, N-terminal	Domain
A, B	IPR013968	Polyketide synthase, ketoreductase domain	Domain
A, B	IPR016039	Thiolase-like	Homologous Superfamily
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR020806	Polyketide synthase, phosphopantetheine-binding domain	Domain
A, B	IPR018201	Beta-ketoacyl synthase, active site	Active Site
A, B	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain	Domain
A, B	IPR036736	ACP-like superfamily	Homologous Superfamily
A, B	IPR042104	Polyketide synthase, dehydratase 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 R01GM133198.