4HSL

2.00 angstrom x-ray crystal structure of substrate-bound E110A 3-hydroxyanthranilate-3,4-dioxygenase from Cupriavidus metallidurans

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	d4hsla_	All beta proteins	Double-stranded beta-helix	RmlC-like cupins	3-hydroxyanthranilic acid dioxygenase-like	3-hydroxyanthranilate-3,4-dioxygenase	(Cupriavidus metallidurans CH34 ) [TaxId: 266264 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	RmlC-like cupins	8034402	3001825	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	3-HAO	e4hslA1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: 3-HAO	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.120.10	Mainly Beta	Sandwich	Jelly Rolls	Jelly Rolls	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF06052	3-hydroxyanthranilic acid dioxygenase (3-HAO)	3-hydroxyanthranilic acid dioxygenase	In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC:1.13.11.6) is part of the kynurenine pathway for the degradation of tryptophan and the biosynthesis of nicotinic acid [1].The prokaryotic homolog is involved in the 2-nitrobenzoate degradation p ...	In eukaryotes 3-hydroxyanthranilic acid dioxygenase (EC:1.13.11.6) is part of the kynurenine pathway for the degradation of tryptophan and the biosynthesis of nicotinic acid [1].The prokaryotic homolog is involved in the 2-nitrobenzoate degradation pathway [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	3-hydroxyanthranilate 3,4-dioxygenase	cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen oxidoreductase activity oxidoreductase activity, acting on single donors with incorporation of molecular oxygen catalytic activity 3-hydroxyanthranilate 3,4-dioxygenase activity dioxygenase activity	quinolinate metabolic process small molecule biosynthetic process oxoacid metabolic process dicarboxylic acid metabolic process pyridine-containing compound biosynthetic process carboxylic acid metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process quinolinate biosynthetic process biosynthetic process pyridine-containing compound metabolic process metabolic process cellular process quinolinate metabolic process small molecule biosynthetic process oxoacid metabolic process dicarboxylic acid metabolic process pyridine-containing compound biosynthetic process carboxylic acid metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process quinolinate biosynthetic process biosynthetic process pyridine-containing compound metabolic process metabolic process cellular process small molecule metabolic process dicarboxylic acid biosynthetic process benzene-containing compound metabolic process aromatic amino acid metabolic process amino acid metabolic process primary metabolic process anthranilate metabolic process monocarboxylic acid metabolic process catabolic process aromatic amino acid family catabolic process indole-containing compound metabolic process organic acid catabolic process alpha-amino acid metabolic process cellular catabolic process carboxylic acid catabolic process indolalkylamine metabolic process amino acid catabolic process amine metabolic process alpha-amino acid catabolic process indole-containing compound catabolic process tryptophan catabolic process small molecule catabolic process biogenic amine metabolic process nucleotide biosynthetic process NAD metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process 'de novo' NAD biosynthetic process phosphate-containing compound metabolic process phosphorus metabolic process pyridine nucleotide metabolic process NAD biosynthetic process pyridine nucleotide biosynthetic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process nucleotide metabolic process nucleobase-containing compound biosynthetic process tryptophan metabolic process L-amino acid metabolic process purine-containing compound metabolic process nicotinamide nucleotide biosynthetic process proteinogenic amino acid metabolic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process 'de novo' NAD biosynthetic process from tryptophan purine nucleotide biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR010329	3-hydroxyanthranilic acid dioxygenase	Family
A	IPR011051	RmlC-like cupin domain superfamily	Homologous Superfamily
A	IPR014710	RmlC-like jelly roll 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.