5E1V

Crystal structure of a monomeric dehydratase domain from a trans AT polyketide synthase split module

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth B]	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8055933	3000149	SCOP2B (2022-06-29)
A [auth B]	SCOP2B Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8055934	3000149	SCOP2B (2022-06-29)
B [auth A]	SCOP2 Family	PKS dehydratase-like	8050558	4006953	SCOP2 (2022-06-29)
B [auth A]	SCOP2 Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8055933	3000149	SCOP2 (2022-06-29)
B [auth A]	SCOP2 Superfamily	Thioesterase/thiol ester dehydrase-isomerase-like	8055934	3000149	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 B]	PF14765	e5e1vB2	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 [auth B]	PF21089	e5e1vB1	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 [auth A]	PF14765	e5e1vA1	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 [auth A]	PF21089	e5e1vA2	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)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth B]	3.10.129.110	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)
B [auth A]	3.10.129.110	Alpha Beta	Roll	Thiol Ester Dehydrase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth A]	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
A [auth B], B [auth A]	PF14765	Polyketide synthase dehydratase N-terminal domain (PS-DH)	Polyketide synthase dehydratase N-terminal domain	This entry represents the N-terminal HotDog domain of the dehydratase (DH) module of polyketide synthases [1]. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and ...	This entry represents the N-terminal HotDog domain of the dehydratase (DH) module of polyketide synthases [1]. Structural analysis shows these DH domains are double hotdogs in which the active site contains a histidine from the N-terminal hotdog and an aspartate from the C-terminal hotdog. Studies have uncovered that a substrate tunnel formed between the DH domains may be essential for loading substrates and unloading products [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth A]	Polyketide synthase PksL	oxidoreductase activity catalytic activity 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 fatty acid synthase activity	antibiotic metabolic process biosynthetic process metabolic process antibiotic biosynthetic process cellular component biogenesis cellular component organization peptidoglycan-based cell wall biogenesis cellular component assembly cell wall biogenesis DIM/DIP cell wall layer assembly cell wall organization or biogenesis cellular process Actinobacterium-type cell wall biogenesis cellular component organization or biogenesis antibiotic metabolic process biosynthetic process metabolic process antibiotic biosynthetic process cellular component biogenesis cellular component organization peptidoglycan-based cell wall biogenesis cellular component assembly cell wall biogenesis DIM/DIP cell wall layer assembly cell wall organization or biogenesis cellular process Actinobacterium-type cell wall biogenesis cellular component organization or biogenesis 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 organic substance biosynthetic process cellular lipid metabolic process small molecule metabolic process monocarboxylic acid metabolic process lipid metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth A]	IPR014031	Beta-ketoacyl synthase, C-terminal	Domain
A [auth B], B [auth A]	IPR006162	Phosphopantetheine attachment site	PTM
A [auth B], B [auth A]	IPR020807	Polyketide synthase, dehydratase domain	Domain
A [auth B], B [auth A]	IPR014030	Beta-ketoacyl synthase, N-terminal	Domain
A [auth B], B [auth A]	IPR049552	Polyketide synthase, dehydratase domain, N-terminal	Domain
A [auth B], B [auth A]	IPR049551	Polyketide synthase, dehydratase domain, C-terminal	Domain
A [auth B], B [auth A]	IPR013968	Polyketide synthase, ketoreductase domain	Domain
A [auth B], B [auth A]	IPR020806	Polyketide synthase, phosphopantetheine-binding domain	Domain
A [auth B], B [auth A]	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain	Domain
A [auth B], B [auth A]	IPR036736	ACP-like superfamily	Homologous Superfamily
A [auth B], B [auth A]	IPR011254	Prismane-like superfamily	Homologous Superfamily
A [auth B], B [auth A]	IPR032821	Polyketide synthase, C-terminal extension	Domain
A [auth B], B [auth A]	IPR009081	Phosphopantetheine binding ACP domain	Domain
A [auth B], B [auth A]	IPR016039	Thiolase-like	Homologous Superfamily
A [auth B], B [auth A]	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A [auth B], B [auth A]	IPR018201	Beta-ketoacyl synthase, active site	Active Site
A [auth B], B [auth A]	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.