3JTK

Crystal Structure of human type-I N-myristoyltransferase with bound myristoyl-CoA and inhibitor DDD90055

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
Pharos: Disease Associations

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d3jtkb1	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d3jtka1	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	automated matches	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8032315	3000403	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8032317	3000403	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8032315	3000403	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8032317	3000403	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	NMT	e3jtkB2	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)
B	NMT_C	e3jtkB1	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)
A	NMT	e3jtkA2	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	e3jtkA1	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)
B	3.40.630.170	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase		CATH (4.3.0)
A	3.40.630.170	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	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, B	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, B	Glycylpeptide N-tetradecanoyltransferase 1	myristoyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity catalytic activity, acting on a protein peptidyl-lysine N6-myristoyltransferase activity glycylpeptide N-tetradecanoyltransferase activity N-acyltransferase activity	protein localization regulation of localization establishment of protein localization cellular localization regulation of cellular process regulation of protein localization positive regulation of biological process positive regulation of establishment of protein localization localization cellular macromolecule localization positive regulation of cellular process regulation of biological process biological regulation regulation of establishment of protein localization protein localization regulation of localization establishment of protein localization cellular localization regulation of cellular process regulation of protein localization positive regulation of biological process positive regulation of establishment of protein localization localization cellular macromolecule localization positive regulation of cellular process regulation of biological process biological regulation regulation of establishment of protein localization establishment of localization regulation of establishment of protein localization to mitochondrion establishment of protein localization to organelle regulation of cellular localization macromolecule localization protein localization to organelle positive regulation of protein localization protein localization to mitochondrion cellular process establishment of protein localization to mitochondrion positive regulation of establishment of protein localization to mitochondrion 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 peptidyl-glycine modification macromolecule modification peptidyl-amino acid modification metabolic process N-terminal peptidyl-glycine N-myristoylation protein metabolic process macromolecule metabolic process protein modification process ketone metabolic process localization within membrane protein localization to membrane cellular response to stimulus response to light stimulus response to stimulus regulation of response to external stimulus signaling regulation of opsin-mediated signaling pathway regulation of signal transduction detection of abiotic stimulus cellular response to environmental stimulus cell communication cellular response to light stimulus signal transduction regulation of G protein-coupled receptor signaling pathway detection of light stimulus phototransduction detection of external stimulus regulation of signaling detection of visible light response to external stimulus cellular response to radiation detection of stimulus regulation of response to stimulus regulation of cell communication response to radiation response to abiotic stimulus G protein-coupled receptor signaling pathway cellular response to abiotic stimulus G protein-coupled opsin signaling pathway phototransduction, visible light developmental process multicellular organism development multicellular organismal process embryo development ending in birth or egg hatching chordate embryonic development anatomical structure development embryo development in utero embryonic development	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

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

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P30419	astrocytic tumor glioblastoma malignant glioma ovarian cancer atypical teratoid rhabdoid tumor hypertensive disorder medulloblastoma primitive neuroectodermal tumor dermatomyositis lung cancer osteosarcoma psoriasis

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.