3TZZ

Crystal structure of a fragment containing the acyltransferase domain of Pks13 from Mycobacterium tuberculosis in the carboxypalmitoylated form at 2.5 A

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Acyl_transf_1_2nd_1	e3tzzA2	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: Acyl_transf_1_2nd_1	ECOD (1.6)
A	PksD_2	e3tzzA3	A: a+b two layers	X: KS-MAT linker domain in fatty acid synthase (From Topology)	H: KS-MAT linker domain in fatty acid synthase (From Topology)	T: KS-MAT linker domain in fatty acid synthase	F: PksD_2	ECOD (1.6)
A	Acyl_transf_1_1st	e3tzzA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: Acyl_transf_1_1st	ECOD (1.6)
B	Acyl_transf_1_2nd_1	e3tzzB2	A: a+b two layers	X: Alpha-beta plaits	H: Probable ACP-binding domain of malonyl-CoA ACP transacylase (From Topology)	T: Probable ACP-binding domain of malonyl-CoA ACP transacylase	F: Acyl_transf_1_2nd_1	ECOD (1.6)
B	PksD_2	e3tzzB3	A: a+b two layers	X: KS-MAT linker domain in fatty acid synthase (From Topology)	H: KS-MAT linker domain in fatty acid synthase (From Topology)	T: KS-MAT linker domain in fatty acid synthase	F: PksD_2	ECOD (1.6)
B	Acyl_transf_1_1st	e3tzzB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: FabD/lysophospholipase-like	F: Acyl_transf_1_1st	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.366.10	Alpha Beta	3-Layer(aba) Sandwich	Malonyl-Coenzyme A Acyl Carrier Protein	domain 2	CATH (4.3.0)
A	3.30.70.250	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Malonyl-CoA ACP transacylase, ACP-binding	CATH (4.3.0)
B	3.40.366.10	Alpha Beta	3-Layer(aba) Sandwich	Malonyl-Coenzyme A Acyl Carrier Protein	domain 2	CATH (4.3.0)
B	3.30.70.250	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Malonyl-CoA ACP transacylase, ACP-binding	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00698	Acyl transferase domain (Acyl_transf_1)	Acyl transferase domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Polyketide synthase PKS13	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 elongation, saturated fatty acid fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process fatty acid elongation carboxylic acid biosynthetic process biosynthetic process fatty acid elongation, saturated fatty acid fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process lipid biosynthetic process primary metabolic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process fatty acid elongation carboxylic acid biosynthetic process biosynthetic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process lipid metabolic process cell wall organization or biogenesis cellular component biogenesis mycolic acid biosynthetic process Actinobacterium-type cell wall biogenesis cellular component organization or biogenesis peptidoglycan-based cell wall biogenesis mycolic acid metabolic process macromolecule biosynthetic process cell wall biogenesis cell wall macromolecule biosynthetic process macromolecule metabolic process mycolate cell wall layer assembly cellular component organization cellular component assembly protein-containing complex organization protein complex oligomerization protein-containing complex assembly protein homooligomerization	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane external encapsulating structure cell wall peptidoglycan-based cell wall protein-containing complex catalytic complex polyketide synthase complex
C	12-mer peptide	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR016035	Acyl transferase/acyl hydrolase/lysophospholipase	Homologous Superfamily
A, B	IPR014031	Beta-ketoacyl synthase, C-terminal	Domain
A, B	IPR053778	Polyketide synthase Pks13	Family
A, B	IPR016036	Malonyl-CoA ACP transacylase, ACP-binding	Homologous Superfamily
A, B	IPR050091	Polyketide and Nonribosomal Peptide Biosynthesis Enzymes	Family
A, B	IPR020806	Polyketide synthase, phosphopantetheine-binding domain	Domain
A, B	IPR020841	Polyketide synthase, beta-ketoacyl synthase domain	Domain
A, B	IPR036736	ACP-like superfamily	Homologous Superfamily
A, B	IPR014043	Acyl transferase domain	Domain
A, B	IPR032821	Polyketide synthase, C-terminal extension	Domain
A, B	IPR009081	Phosphopantetheine binding ACP domain	Domain
A, B	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily
A, B	IPR016039	Thiolase-like	Homologous Superfamily
A, B	IPR001227	Acyl transferase domain superfamily	Homologous Superfamily
A, B	IPR018201	Beta-ketoacyl synthase, active site	Active Site
A, B	IPR014030	Beta-ketoacyl synthase-like, N-terminal	Domain
A, B	IPR001031	Thioesterase	Domain

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.