3IMG

Crystal Structure of Mycobacterium Tuberculosis Pantothenate Synthetase at 1.8 Ang resolution in a ternary complex with fragment compounds 5-methoxyindole and 1-benzofuran-2-carboxylic acid

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)
B	d3imgb_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Nucleotidylyl transferase	Pantothenate synthetase (Pantoate-beta-alanine ligase, PanC)	Pantothenate synthetase (Pantoate-beta-alanine ligase, PanC)	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)
A	d3imga_	Alpha and beta proteins (a/b)	Adenine nucleotide alpha hydrolase-like	Nucleotidylyl transferase	Pantothenate synthetase (Pantoate-beta-alanine ligase, PanC)	Pantothenate synthetase (Pantoate-beta-alanine ligase, PanC)	(Mycobacterium tuberculosis ) [TaxId: 1773 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Nucleotidylyl transferase	8040229	3001541	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Nucleotidylyl transferase	8040229	3001541	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	Pantoate_ligase_C	e3imgB2	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: Pantoate_ligase_C	ECOD (1.6)
B	Pantoate_ligase_N	e3imgB3	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_C	e3imgA1	A: a+b duplicates or obligate multimers	X: Creatinase/aminopeptidase-like	H: Creatinase/aminopeptidase (From Topology)	T: Creatinase/aminopeptidase	F: Pantoate_ligase_C	ECOD (1.6)
A	Pantoate_ligase_N	e3imgA2	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)
B	3.30.1300.10	Alpha Beta	2-Layer Sandwich	Pantoate--beta-alanine Ligase	Chain: A,domain 2	CATH (4.3.0)
A	3.40.50.620	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	HUPs	CATH (4.3.0)
A	3.30.1300.10	Alpha Beta	2-Layer Sandwich	Pantoate--beta-alanine Ligase	Chain: A,domain 2	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	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding manganese ion binding transition metal ion binding acid-amino acid ligase activity pantoate-beta-alanine ligase activity catalytic activity ligase activity, forming carbon-nitrogen bonds ligase activity	non-proteinogenic amino acid metabolic process beta-alanine metabolic process oxoacid metabolic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process metabolic process cellular process small molecule metabolic process organic acid metabolic process pantothenate metabolic process water-soluble vitamin biosynthetic process monocarboxylic acid biosynthetic process small molecule biosynthetic process non-proteinogenic amino acid metabolic process beta-alanine metabolic process oxoacid metabolic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process metabolic process cellular process small molecule metabolic process organic acid metabolic process pantothenate metabolic process water-soluble vitamin biosynthetic process monocarboxylic acid biosynthetic process small molecule biosynthetic process modified amino acid biosynthetic process modified amino acid metabolic process vitamin biosynthetic process amide biosynthetic process organic acid biosynthetic process carboxylic acid biosynthetic process vitamin metabolic process biosynthetic process pantothenate biosynthetic 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	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.