3GUZ

Structural and substrate-binding studies of pantothenate synthenate (PS)provide insights into homotropic inhibition by pantoate in PS's

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	Pantoate_ligase_N	e3guzB1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Pantoate_ligase_N	ECOD (1.6)
A	Pantoate_ligase_N	e3guzA1	A: a/b three-layered sandwiches	X: HUP domain-like	H: HUP domains (From Topology)	T: HUP domains	F: Pantoate_ligase_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
A	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02569	Pantoate-beta-alanine ligase (Pantoate_ligase)	Pantoate-beta-alanine ligase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Pantothenate synthetase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding acid-amino acid ligase activity pantoate-beta-alanine ligase activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity identical protein binding protein binding protein homodimerization activity protein dimerization activity	pantothenate metabolic process water-soluble vitamin biosynthetic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process modified amino acid biosynthetic process carboxylic acid metabolic process modified amino acid metabolic process vitamin biosynthetic process amide biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process vitamin metabolic process biosynthetic process pantothenate metabolic process water-soluble vitamin biosynthetic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process modified amino acid biosynthetic process carboxylic acid metabolic process modified amino acid metabolic process vitamin biosynthetic process amide biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process vitamin metabolic process biosynthetic process pantothenate biosynthetic process small molecule metabolic process metabolic process cellular process monocarboxylic acid metabolic process amide metabolic process water-soluble vitamin metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR004821	Cytidyltransferase-like domain	Domain
A, B	IPR042176	Pantoate-beta-alanine ligase, C-terminal domain	Homologous Superfamily
A, B	IPR003721	Pantoate-beta-alanine ligase	Family
A, B	IPR014729	Rossmann-like alpha/beta/alpha sandwich fold	Homologous Superfamily

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.