Annotations: 3JQY

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B [auth A]	F_UNCLASSIFIED	e3jqyA1	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: F_UNCLASSIFIED	ECOD (1.6)
A [auth B]	F_UNCLASSIFIED	e3jqyB2	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: F_UNCLASSIFIED	ECOD (1.6)
C	F_UNCLASSIFIED	e3jqyC2	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: F_UNCLASSIFIED	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth A]	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (4.3.0)
A [auth B]	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (4.3.0)
C	2.160.10.10	Mainly Beta	3 Solenoid	UDP N-Acetylglucosamine Acyltransferase	domain 1	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth A], C	Polysialic acid O-acetyltransferase	acetyltransferase activity O-acyltransferase activity acyltransferase activity polysialic-acid O-acetyltransferase activity O-acetyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth A], C	IPR011004	Trimeric LpxA-like superfamily	Homologous Superfamily
A [auth B], B [auth A], C	IPR018357	Hexapeptide transferase, conserved site	Conserved Site

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 R01GM133198.