4ZSI

Crystal structure of the effector-binding domain of DasR (DasR-EBD) in complex with glucosamine-6-phosphate

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	d4zsib_	Alpha and beta proteins (a+b)	Chorismate lyase-like	Chorismate lyase-like	automated matches	automated matches	(Streptomyces coelicolor A3(2) ) [TaxId: 100226 ],	SCOPe (2.08)
A	d4zsia1	Alpha and beta proteins (a+b)	Chorismate lyase-like	Chorismate lyase-like	automated matches	automated matches	(Streptomyces coelicolor A3(2) ) [TaxId: 100226 ],	SCOPe (2.08)
A	d4zsia2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Streptomyces coelicolor A3(2) ) [TaxId: 100226 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Chorismate lyase-like	8059023	3000072	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Chorismate lyase-like	8059023	3000072	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	UTRA	e4zsiB1	A: a+b two layers	X: Chorismate lyase (From Topology)	H: Chorismate lyase (From Topology)	T: Chorismate lyase	F: UTRA	ECOD (1.6)
A	UTRA	e4zsiA1	A: a+b two layers	X: Chorismate lyase (From Topology)	H: Chorismate lyase (From Topology)	T: Chorismate lyase	F: UTRA	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.1410.10	Alpha Beta	3-Layer(aba) Sandwich	Chorismate lyase	Chorismate lyase-like	CATH (4.3.0)
A	3.40.1410.10	Alpha Beta	3-Layer(aba) Sandwich	Chorismate lyase	Chorismate lyase-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF07702	UTRA domain (UTRA)	UTRA domain	The UbiC transcription regulator-associated (UTRA) domain is a conserved ligand-binding domain that has a similar fold to Pfam:PF04345 [1]. It is believed to modulate activity of bacterial transcription factors in response to binding small molecules ...	The UbiC transcription regulator-associated (UTRA) domain is a conserved ligand-binding domain that has a similar fold to Pfam:PF04345 [1]. It is believed to modulate activity of bacterial transcription factors in response to binding small molecules [1] sugar phosphates and urocanate, Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	HTH-type transcriptional repressor DasR	DNA binding binding organic cyclic compound binding nucleic acid binding transcription regulator activity DNA-binding transcription factor activity	regulation of cellular process negative regulation of biological process RNA metabolic process regulation of primary metabolic process negative regulation of RNA biosynthetic process RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription nucleic acid biosynthetic process regulation of RNA metabolic process negative regulation of cellular process negative regulation of nucleobase-containing compound metabolic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process regulation of cellular process negative regulation of biological process RNA metabolic process regulation of primary metabolic process negative regulation of RNA biosynthetic process RNA biosynthetic process nucleobase-containing compound metabolic process DNA-templated transcription nucleic acid biosynthetic process regulation of RNA metabolic process negative regulation of cellular process negative regulation of nucleobase-containing compound metabolic process regulation of nucleobase-containing compound metabolic process regulation of RNA biosynthetic process negative regulation of macromolecule metabolic process regulation of biosynthetic process negative regulation of DNA-templated transcription regulation of biological process negative regulation of metabolic process biological regulation primary metabolic process regulation of macromolecule metabolic process nucleobase-containing compound biosynthetic process gene expression macromolecule biosynthetic process nucleic acid metabolic process regulation of gene expression biosynthetic process negative regulation of biosynthetic process negative regulation of macromolecule biosynthetic process metabolic process cellular process regulation of macromolecule biosynthetic process macromolecule metabolic process regulation of DNA-templated transcription regulation of metabolic process negative regulation of RNA metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR050679	Bacterial HTH-type transcriptional regulator	Family
A, B	IPR011663	UbiC transcription regulator-associated	Domain
A, B	IPR028978	Chorismate pyruvate-lyase/UbiC transcription regulator-associated domain superfamily	Homologous Superfamily
A, B	IPR036388	Winged helix-like DNA-binding domain superfamily	Homologous Superfamily
A, B	IPR000524	Transcription regulator HTH, GntR	Domain
A, B	IPR036390	Winged helix DNA-binding domain superfamily	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.