2VEZ

AfGNA1 crystal structure complexed with Acetyl-CoA and Glucose-6P gives new insights into catalysis

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2veza_	Alpha and beta proteins (a+b)	Acyl-CoA N-acyltransferases (Nat)	Acyl-CoA N-acyltransferases (Nat)	automated matches	automated matches	SARTORYA FUMIGATA (Aspergillus fumigatus ) [TaxId: 746128 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	N-acetyltransferase, NAT	8081161	4001800	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Acyl-CoA N-acyltransferases (Nat)	8081162	3000403	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Acetyltransf_10_2	e2vezA1	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_2	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	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	PUTATIVE GLUCOSAMINE 6-PHOSPHATE ACETYLTRANSFERASE	glucosamine 6-phosphate N-acetyltransferase activity acetyltransferase activity N-acetyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity N-acyltransferase activity	amino sugar biosynthetic process carbohydrate derivative metabolic process UDP-N-acetylglucosamine biosynthetic process nucleobase-containing compound metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process amino sugar metabolic process small molecule metabolic process nucleotide-sugar biosynthetic process phosphorus metabolic process UDP-N-acetylglucosamine metabolic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process cellular metabolic process amino sugar biosynthetic process carbohydrate derivative metabolic process UDP-N-acetylglucosamine biosynthetic process nucleobase-containing compound metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process amino sugar metabolic process small molecule metabolic process nucleotide-sugar biosynthetic process phosphorus metabolic process UDP-N-acetylglucosamine metabolic process nucleoside phosphate metabolic process carbohydrate derivative biosynthetic process cellular metabolic process nucleotide-sugar metabolic process primary metabolic process nucleobase-containing compound biosynthetic process biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process metabolic process cellular process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR016181	Acyl-CoA N-acyltransferase	Homologous Superfamily
A	IPR000182	GNAT domain	Domain
A	IPR039143	Glucosamine 6-phosphate N-acetyltransferase-like	Family

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.