1KPG

Crystal Structure of mycolic acid cyclopropane synthase CmaA1 complexed with SAH and CTAB

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)
B	d1kpgb_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	Mycolic acid cyclopropane synthase	CmaA1	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
A	d1kpga_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	Mycolic acid cyclopropane synthase	CmaA1	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
C	d1kpgc_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	Mycolic acid cyclopropane synthase	CmaA1	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
D	d1kpgd_	Alpha and beta proteins (a/b)	S-adenosyl-L-methionine-dependent methyltransferases	S-adenosyl-L-methionine-dependent methyltransferases	Mycolic acid cyclopropane synthase	CmaA1	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	S-adenosyl-L-methionine-dependent methyltransferases	8038339	3000118	SCOP2B (2022-06-29)
A	SCOP2 Family	Mycolic acid cyclopropane synthase	8025960	4003320	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	S-adenosyl-L-methionine-dependent methyltransferases	8038339	3000118	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	S-adenosyl-L-methionine-dependent methyltransferases	8038339	3000118	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	S-adenosyl-L-methionine-dependent methyltransferases	8038339	3000118	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)
B	CMAS	e1kpgB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: CMAS	ECOD (1.6)
A	CMAS	e1kpgA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: CMAS	ECOD (1.6)
C	CMAS	e1kpgC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: CMAS	ECOD (1.6)
D	CMAS	e1kpgD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: CMAS	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
A	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
C	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)
D	3.40.50.150	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Vaccinia Virus protein VP39	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF02353	Mycolic acid cyclopropane synthetase (CMAS)	Mycolic acid cyclopropane synthetase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	CYCLOPROPANE-FATTY-ACYL-PHOSPHOLIPID SYNTHASE 1	cyclopropane-fatty-acyl-phospholipid synthase activity transferase activity, transferring one-carbon groups transferase activity methyltransferase activity S-adenosylmethionine-dependent methyltransferase activity catalytic activity	methylation metabolic process cellular process S-adenosylmethionine metabolic process sulfur compound metabolic process oxoacid metabolic process cell wall organization or biogenesis lipid biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process cellular component biogenesis mycolic acid biosynthetic process Actinobacterium-type cell wall biogenesis methylation metabolic process cellular process S-adenosylmethionine metabolic process sulfur compound metabolic process oxoacid metabolic process cell wall organization or biogenesis lipid biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process cellular component biogenesis mycolic acid biosynthetic process Actinobacterium-type cell wall biogenesis small molecule metabolic process cellular component organization or biogenesis peptidoglycan-based cell wall biogenesis fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process mycolic acid metabolic process carboxylic acid metabolic process primary metabolic process fatty acid biosynthetic process macromolecule biosynthetic process cell wall biogenesis biosynthetic process cell wall macromolecule biosynthetic process macromolecule metabolic process monocarboxylic acid metabolic process lipid metabolic process	cell periphery cellular anatomical structure plasma membrane membrane intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily	Homologous Superfamily
A, B, C, D	IPR003333	Cyclopropane mycolic acid synthase	Family
A, B, C, D	IPR047672	Cyclopropane mycolic acid synthase, actinobacteria	Family
A, B, C, D	IPR050723	Cyclopropane Fatty Acid Synthase/Methyltransferase	Family

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.