4INE

Crystal structure of N-methyl transferase (PMT-2) from Caenorhabditis elegant complexed with S-adenosyl homocysteine and phosphoethanolamine

External Resource: Annotation

Domain Annotation: ECOD Classification
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	Methyltransf_11_like	e4ineA1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: Methyltransf_11_like	ECOD (1.6)
A	Methyltransf_11	e4ineA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: Methyltransf_11	ECOD (1.6)
B	Methyltransf_11_like	e4ineB1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: Methyltransf_11_like	ECOD (1.6)
B	Methyltransf_11	e4ineB2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: S-adenosyl-L-methionine-dependent methyltransferases	F: Methyltransf_11	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF08241	Methyltransferase domain (Methyltransf_11)	Methyltransferase domain	Members of this family are SAM dependent methyltransferases.	Domain
A, B	PF17987	Phosphoethanolamine N-methyltransferase 2 N-terminal (PMT2_N)	Phosphoethanolamine N-methyltransferase 2 N-terminal	This is the N-terminal vestigial domain found in Haemonchus contortus phosphoethanolamine N-methyltransferases 2 (PMT2). Structural analysis reveal changes leading to loss of function in the vestigial domains of the nematode PMT [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Protein PMT-2	phosphoethanolamine N-methyltransferase activity transferase activity, transferring one-carbon groups N-methyltransferase activity transferase activity methyltransferase activity catalytic activity S-adenosylmethionine-dependent methyltransferase activity phosphomethylethanolamine N-methyltransferase activity phosphatidyl-N-dimethylethanolamine N-methyltransferase activity phosphatidyl-N-methylethanolamine N-methyltransferase activity	methylation metabolic process cellular biosynthetic process glycerophospholipid metabolic process organonitrogen compound biosynthetic process lipid biosynthetic process phospholipid metabolic process organic substance metabolic process phosphate-containing compound metabolic process organic substance biosynthetic process phosphatidylcholine metabolic process phosphorus metabolic process organonitrogen compound metabolic process glycerophospholipid biosynthetic process methylation metabolic process cellular biosynthetic process glycerophospholipid metabolic process organonitrogen compound biosynthetic process lipid biosynthetic process phospholipid metabolic process organic substance metabolic process phosphate-containing compound metabolic process organic substance biosynthetic process phosphatidylcholine metabolic process phosphorus metabolic process organonitrogen compound metabolic process glycerophospholipid biosynthetic process cellular metabolic process primary metabolic process phospholipid biosynthetic process biosynthetic process glycerolipid biosynthetic process organophosphate metabolic process organophosphate biosynthetic process cellular lipid metabolic process glycerolipid metabolic process cellular process phosphatidylcholine biosynthetic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR040516	Phosphoethanolamine N-methyltransferase 2, N-terminal	Domain
A, B	IPR029063	S-adenosyl-L-methionine-dependent methyltransferase superfamily	Homologous Superfamily
A, B	IPR013216	Methyltransferase type 11	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.