7KD7

Crystal structure of human NatD (NAA40) bound to a bisubstrate analogue

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth D]	Acetyltransf_10_3	e7kd7D1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_10_3	ECOD (1.6)
C [auth A]	Acetyltransf_10_3	e7kd7A1	A: a+b three layers	X: Nat/Ivy	H: Acyl-CoA N-acyltransferases (Nat) (From Topology)	T: Acyl-CoA N-acyltransferases (Nat)	F: Acetyltransf_10_3	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth D], C [auth A]	PF00583	Acetyltransferase (GNAT) family (Acetyltransf_1)	Acetyltransferase (GNAT) family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B [auth E], D [auth B]	SER-GLY-ARG-GLY-LYS	-	-	-
A [auth D], C [auth A]	N-alpha-acetyltransferase 40	catalytic activity, acting on a protein histone H2A acetyltransferase activity N-acetyltransferase activity acyltransferase activity transferase activity peptide N-acetyltransferase activity histone acetyltransferase activity acetyltransferase activity peptide-lysine-N-acetyltransferase activity histone modifying activity acyltransferase activity, transferring groups other than amino-acyl groups catalytic activity N-acyltransferase activity peptide-serine-alpha-N-acetyltransferase activity catalytic activity, acting on a protein histone H2A acetyltransferase activity N-acetyltransferase activity acyltransferase activity transferase activity peptide N-acetyltransferase activity histone acetyltransferase activity acetyltransferase activity peptide-lysine-N-acetyltransferase activity histone modifying activity acyltransferase activity, transferring groups other than amino-acyl groups catalytic activity N-acyltransferase activity peptide-serine-alpha-N-acetyltransferase activity peptide alpha-N-acetyltransferase activity histone H4 acetyltransferase activity	primary metabolic process metabolic process cellular process lipid metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen cellular anatomical structure intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle nucleus membrane-enclosed lumen intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle nucleoplasm organelle lumen organelle nuclear lumen intracellular membraneless organelle centrosome microtubule organizing center cytoskeleton centriolar satellite membraneless organelle microtubule cytoskeleton

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth D], C [auth A]	IPR016181	Acyl-CoA N-acyltransferase	Homologous Superfamily
A [auth D], C [auth A]	IPR039949	N-alpha-acetyltransferase 40	Family
A [auth D], C [auth A]	IPR000182	GNAT domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A [auth D], C [auth A]	Pharos: Q86UY6	adenoma endogenous depression malignant mesothelioma ovarian cancer psoriasis astrocytic tumor lung cancer medulloblastoma pancreatic intraductal papillary-mucinous neoplasm bipolar disorder malignant colon neoplasm osteosarcoma primitive neuroectodermal tumor

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.