6F7F

Tryptophan Repressor TrpR from E.coli with 3-Indolepropionic 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)
C [auth D]	d6f7fd_	All alpha proteins	DNA/RNA-binding 3-helical bundle	TrpR-like	Trp repressor, TrpR	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D [auth C]	d6f7fc_	All alpha proteins	DNA/RNA-binding 3-helical bundle	TrpR-like	Trp repressor, TrpR	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A [auth B]	d6f7fb_	All alpha proteins	DNA/RNA-binding 3-helical bundle	TrpR-like	Trp repressor, TrpR	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B [auth A]	d6f7fa_	All alpha proteins	DNA/RNA-binding 3-helical bundle	TrpR-like	Trp repressor, TrpR	automated matches	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C [auth D]	SCOP2B Superfamily	TrpR-like	8038304	3001097	SCOP2B (2022-06-29)
D [auth C]	SCOP2B Superfamily	TrpR-like	8038304	3001097	SCOP2B (2022-06-29)
A [auth B]	SCOP2B Superfamily	TrpR-like	8038304	3001097	SCOP2B (2022-06-29)
B [auth A]	SCOP2B Superfamily	TrpR-like	8038304	3001097	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)
C [auth D]	Trp_repressor	e6f7fD1	A: alpha arrays	X: HTH	H: HTH	T: TrpR	F: Trp_repressor	ECOD (1.6)
D [auth C]	Trp_repressor	e6f7fC1	A: alpha arrays	X: HTH	H: HTH	T: TrpR	F: Trp_repressor	ECOD (1.6)
A [auth B]	Trp_repressor	e6f7fB1	A: alpha arrays	X: HTH	H: HTH	T: TrpR	F: Trp_repressor	ECOD (1.6)
B [auth A]	Trp_repressor	e6f7fA1	A: alpha arrays	X: HTH	H: HTH	T: TrpR	F: Trp_repressor	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C [auth D]	1.10.1270.10	Mainly Alpha	Orthogonal Bundle	Trp Operon Repressor	Chain A	CATH (utative)
D [auth C]	1.10.1270.10	Mainly Alpha	Orthogonal Bundle	Trp Operon Repressor	Chain A	CATH (utative)
A [auth B]	1.10.1270.10	Mainly Alpha	Orthogonal Bundle	Trp Operon Repressor	Chain A	CATH (utative)
B [auth A]	1.10.1270.10	Mainly Alpha	Orthogonal Bundle	Trp Operon Repressor	Chain A	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth A], C [auth D], D [auth C]	PF01371	Trp repressor protein (Trp_repressor)	Trp repressor protein	This protein binds to tryptophan and represses transcription of the Trp operon.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth A], C [auth D], D [auth C]	Trp operon repressor	DNA binding binding organic cyclic compound binding nucleic acid binding transcription regulator activity DNA-binding transcription factor activity sequence-specific DNA binding	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 [auth B], B [auth A], C [auth D], D [auth C]	IPR038116	TrpR-like superfamily	Homologous Superfamily
A [auth B], B [auth A], C [auth D], D [auth C]	IPR000831	Trp repressor	Family
A [auth B], B [auth A], C [auth D], D [auth C]	IPR013335	Trp repressor, bacterial	Family
A [auth B], B [auth A], C [auth D], D [auth C]	IPR010921	Trp repressor/replication initiator	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.