2IV3

Crystal structure of AviGT4, a glycosyltransferase involved in Avilamycin A biosynthesis

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)
B	Glycos_transf_1	e2iv3B1	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: Glycos_transf_1	ECOD (1.6)
B	Glyco_transf_4	e2iv3B2	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: Glyco_transf_4	ECOD (1.6)
C	Glycos_transf_1	e2iv3C1	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: Glycos_transf_1	ECOD (1.6)
C	Glyco_transf_4	e2iv3C2	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: Glyco_transf_4	ECOD (1.6)
A	Glycos_transf_1	e2iv3A1	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: Glycos_transf_1	ECOD (1.6)
A	Glyco_transf_4	e2iv3A2	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: Glyco_transf_4	ECOD (1.6)
D	Glycos_transf_1	e2iv3D1	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: Glycos_transf_1	ECOD (1.6)
D	Glyco_transf_4	e2iv3D2	A: a/b three-layered sandwiches	X: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	H: UDP-Glycosyltransferase/glycogen phosphorylase (From Topology)	T: UDP-Glycosyltransferase/glycogen phosphorylase	F: Glyco_transf_4	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.2000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycogen Phosphorylase B	CATH (4.3.0)
C	3.40.50.2000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycogen Phosphorylase B	CATH (4.3.0)
A	3.40.50.2000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycogen Phosphorylase B	CATH (4.3.0)
D	3.40.50.2000	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycogen Phosphorylase B	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00534	Glycosyl transferases group 1 (Glycos_transf_1)	Glycosyl transferases group 1	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	GLYCOSYLTRANSFERASE	glycosyltransferase activity transferase activity catalytic activity binding nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR001296	Glycosyl transferase, family 1	Domain

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.