4EAA

X-ray crystal structure of the H141N mutant of perosamine N-acetyltransferase from Caulobacter crescentus in complex with CoA and GDP-perosamine

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Hexapep_2_1	e4eaaA5	A: beta duplicates or obligate multimers	X: Single-stranded left-handed beta-helix	H: Trimeric LpxA-like enzymes (From Topology)	T: Trimeric LpxA-like enzymes	F: Hexapep_2_1	ECOD (1.6)
A	NeuD_NnaD	e4eaaA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: MurCD/PglD N-terminal domain-like	F: NeuD_NnaD	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.20	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
A	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF17836	PglD N-terminal domain (PglD_N)	PglD N-terminal domain	This alpha/beta domain is found at the N-terminus of proteins such as PglD [2]. This domain binds a UDP-sugar substrate [3].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Perosamine N-acetyltransferase	transferase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR011004	Trimeric LpxA-like superfamily	Homologous Superfamily
A	IPR041561	PglD, N-terminal	Domain
A	IPR050179	Transferase hexapeptide repeat	Family
A	IPR020019	Acyltransferase PglD-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.