6WF3

Crystal structure of human Naa50 in complex with a cofactor derived inhibitor (compound 1)

External Resource: Annotation

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
Protein Modification Annotation

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)	8087499	3000403	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8087499	3000403	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8087499	3000403	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8087499	3000403	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8087499	3000403	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Acyl-CoA N-acyltransferases (Nat)	8087499	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	Acetyltransf_10_3	e6wf3B1	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)
D	Acetyltransf_10_3	e6wf3D1	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)
E	Acetyltransf_10_3	e6wf3E1	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)
F	Acetyltransf_10_3	e6wf3F1	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)
A	Acetyltransf_10_3	e6wf3A1	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	Acetyltransf_10_3	e6wf3C1	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)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (utative)
D	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (utative)
E	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (utative)
F	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (utative)
A	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (utative)
C	3.40.630.30	Alpha Beta	3-Layer(aba) Sandwich	Aminopeptidase	Gcn5-related N-acetyltransferase (GNAT)	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	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
A, B, C, D, E A, B, C, D, E, F	N-alpha-acetyltransferase 50	acetyltransferase activity N-acetyltransferase activity acyltransferase activity peptide alpha-N-acetyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity peptide N-acetyltransferase activity catalytic activity N-acyltransferase activity catalytic activity, acting on a protein histone H4 acetyltransferase activity histone acetyltransferase activity peptide-lysine-N-acetyltransferase activity histone modifying activity	primary metabolic process gene expression macromolecule biosynthetic process protein acylation protein maturation protein acetylation biosynthetic process N-terminal protein amino acid modification macromolecule modification N-terminal protein amino acid acetylation metabolic process cellular process protein metabolic process macromolecule metabolic process primary metabolic process gene expression macromolecule biosynthetic process protein acylation protein maturation protein acetylation biosynthetic process N-terminal protein amino acid modification macromolecule modification N-terminal protein amino acid acetylation metabolic process cellular process protein metabolic process macromolecule metabolic process protein modification process cellular component organization organelle organization mitotic sister chromatid cohesion chromosome organization sister chromatid cohesion cellular component organization or biogenesis cell cycle cell cycle process establishment of mitotic sister chromatid cohesion mitotic cell cycle mitotic cell cycle process establishment of sister chromatid cohesion centromeric sister chromatid cohesion mitotic sister chromatid cohesion, centromeric	membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membraneless organelle intracellular membrane-bounded organelle nucleolus intracellular organelle lumen intracellular organelle cellular anatomical structure organelle lumen organelle membraneless organelle nuclear lumen membrane-bounded organelle intracellular anatomical structure nucleus membrane-enclosed lumen intracellular membraneless organelle intracellular membrane-bounded organelle nucleolus intracellular organelle lumen intracellular organelle cellular anatomical structure organelle lumen organelle membraneless organelle nuclear lumen extracellular exosome extracellular vesicle extracellular organelle extracellular region extracellular space vesicle extracellular membrane-bounded organelle cytoplasm cytosol protein-containing complex NatA complex catalytic complex N-terminal protein acetyltransferase complex transferase complex acetyltransferase complex protein acetyltransferase complex intracellular protein-containing complex
G, H, I, J, K G, H, I, J, K, L	ACE-MET-LEU-GLY-PRO-NH2	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR000182	GNAT domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR051556	N-terminal and lysine N-acetyltransferase	Family
A, B, C, D, E A, B, C, D, E, F	IPR016181	Acyl-CoA N-acyltransferase	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F	Pharos: Q9GZZ1	pancreatic intraductal papillary-mucinous neoplasm atopic eczema cystic fibrosis gastric carcinoma hereditary spastic paraplegia malignant glioma medulloblastoma osteosarcoma plasma cell myeloma atypical teratoid rhabdoid tumor exocrine pancreatic carcinoma glioblastoma large cell medulloblastoma malignant mesothelioma non-small cell lung carcinoma pancreatic intraductal papillary-mucinous neoplasm atopic eczema cystic fibrosis gastric carcinoma hereditary spastic paraplegia malignant glioma medulloblastoma osteosarcoma plasma cell myeloma atypical teratoid rhabdoid tumor exocrine pancreatic carcinoma glioblastoma large cell medulloblastoma malignant mesothelioma non-small cell lung carcinoma ovarian cancer tuberculosis breast cancer gastric cancer hepatocellular carcinoma lung cancer malignant pancreatic neoplasm Ogden syndrome

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
G, H, I, J, K G, H, I, J, K, L	ACE	RESID: AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 PSI-MOD : N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359
G, H, I, J, K G, H, I, J, K, L	NH2	RESID: AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 , AA0081 , AA0083 , AA0084 , AA0086 , AA0087 , AA0088 , AA0090 , AA0091 , AA0092 , AA0093 , AA0095 , AA0096 , AA0097 , AA0098 , AA0099 , AA0100 PSI-MOD : N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359 , L-alanine amide MOD:00090 , L-asparagine amide MOD:00092 , L-aspartic acid 1-amide MOD:00093 , L-glutamine amide MOD:00095 , L-glutamic acid 1-amide MOD:00096 , glycine amide MOD:00097 , L-isoleucine amide MOD:00099 , L-leucine amide MOD:00100 , L-lysine amide MOD:00101 , L-methionine amide MOD:00102 , L-proline amide MOD:00104 , L-serine amide MOD:00105 , L-threonine amide MOD:00106 , L-tryptophan amide MOD:00107 , L-tyrosine amide MOD:00108 , L-valine amide MOD:00109

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.