5T6E

Crystal structure of Aspergillus fumigatus N-myristoyl transferase in complex with myristoyl CoA and a dichloro-dimethylpyridyl-methoxy-phenyl-pyridyl-piperazine ligand

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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)
A	d5t6ea1	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	automated matches	automated matches	(Aspergillus fumigatus Af293 ) [TaxId: 330879 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	NMT	e5t6eA1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: NMT	ECOD (1.6)
A	NMT_C	e5t6eA2	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: NMT_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01233	Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain (NMT)	Myristoyl-CoA:protein N-myristoyltransferase, N-terminal domain	The N and C-terminal domains of NMT are structurally similar, each adopting an acyl-CoA N-acyltransferase-like fold.	Domain
A	PF02799	Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain (NMT_C)	Myristoyl-CoA:protein N-myristoyltransferase, C-terminal domain	The N and C-terminal domains of NMT are structurally similar, each adopting an acyl-CoA N-acyltransferase-like fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Glycylpeptide N-tetradecanoyltransferase	acyltransferase activity myristoyltransferase activity glycylpeptide N-tetradecanoyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity N-acyltransferase activity	lipoprotein biosynthetic process lipoprotein metabolic process primary metabolic process N-terminal protein lipidation macromolecule biosynthetic process N-terminal protein myristoylation protein acylation protein lipidation biosynthetic process protein myristoylation N-terminal protein amino acid modification macromolecule modification metabolic process cellular process lipoprotein biosynthetic process lipoprotein metabolic process primary metabolic process N-terminal protein lipidation macromolecule biosynthetic process N-terminal protein myristoylation protein acylation protein lipidation biosynthetic process protein myristoylation N-terminal protein amino acid modification macromolecule modification metabolic process cellular process protein metabolic process macromolecule metabolic process protein modification process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR016181	Acyl-CoA N-acyltransferase	Homologous Superfamily
A	IPR022677	Glycylpeptide N-tetradecanoyltransferase, C-terminal	Domain
A	IPR022676	Glycylpeptide N-tetradecanoyltransferase, N-terminal	Domain
A	IPR000903	Glycylpeptide N-tetradecanoyltransferase	Family
A	IPR022678	Glycylpeptide N-tetradecanoyltransferase, conserved site	Conserved Site

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.