1LBL

Crystal structure of indole-3-glycerol phosphate synthase (IGPS) in complex with 1-(o-carboxyphenylamino)-1-deoxyribulose 5'-phosphate (CdRP)

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)
A	d1lbla_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Ribulose-phoshate binding barrel	Tryptophan biosynthesis enzymes	Indole-3-glycerophosphate synthase, IPGS	(Saccharolobus solfataricus ) [TaxId: 2287 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Ribulose-phoshate binding barrel	8043259	3000216	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)
A	IGPS	e1lblA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: IGPS	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.70	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Aldolase class I	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00218	Indole-3-glycerol phosphate synthase (IGPS)	Indole-3-glycerol phosphate synthase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	indole-3-glycerol phosphate synthase	indole-3-glycerol-phosphate synthase activity carboxy-lyase activity lyase activity catalytic activity carbon-carbon lyase activity phosphoribosylanthranilate isomerase activity isomerase activity intramolecular oxidoreductase activity, interconverting aldoses and ketoses intramolecular oxidoreductase activity	oxoacid metabolic process cellular biosynthetic process indole-containing compound metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process biogenic amine biosynthetic process tryptophan biosynthetic process indole-containing compound biosynthetic process indolalkylamine metabolic process small molecule metabolic process indolalkylamine biosynthetic process oxoacid metabolic process cellular biosynthetic process indole-containing compound metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process biogenic amine biosynthetic process tryptophan biosynthetic process indole-containing compound biosynthetic process indolalkylamine metabolic process small molecule metabolic process indolalkylamine biosynthetic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process primary metabolic process amine metabolic process amino acid biosynthetic process biosynthetic process amine biosynthetic process metabolic process cellular process biogenic amine metabolic process alpha-amino acid biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR013798	Indole-3-glycerol phosphate synthase domain	Domain
A	IPR011060	Ribulose-phosphate binding barrel	Homologous Superfamily
A	IPR001468	Indole-3-glycerol phosphate synthase, conserved site	Conserved Site
A	IPR013785	Aldolase-type TIM barrel	Homologous Superfamily
A	IPR045186	Indole-3-glycerol phosphate synthase	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.