4RPN

PcpR inducer binding domain complex with pentachlorophenol

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 [auth C]	d4rpnc_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Sphingobium chlorophenolicum ) [TaxId: 46429 ],	SCOPe (2.08)
A [auth D]	d4rpnd_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Sphingobium chlorophenolicum ) [TaxId: 46429 ],	SCOPe (2.08)
C [auth A]	d4rpna_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Sphingobium chlorophenolicum ) [TaxId: 46429 ],	SCOPe (2.08)
D [auth B]	d4rpnb_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Sphingobium chlorophenolicum ) [TaxId: 46429 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B [auth C]	SCOP2B Superfamily	Type 2 solute binding protein-like	8086827	3000083	SCOP2B (2022-06-29)
A [auth D]	SCOP2B Superfamily	Type 2 solute binding protein-like	8086827	3000083	SCOP2B (2022-06-29)
C [auth A]	SCOP2B Superfamily	Type 2 solute binding protein-like	8086827	3000083	SCOP2B (2022-06-29)
D [auth B]	SCOP2B Superfamily	Type 2 solute binding protein-like	8086827	3000083	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 [auth C]	LysR_substrate_2	e4rpnC2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: LysR_substrate_2	ECOD (1.6)
B [auth C]	UNK_F_TYPE	e4rpnC1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: UNK_F_TYPE	ECOD (1.6)
A [auth D]	LysR_substrate_2	e4rpnD1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: LysR_substrate_2	ECOD (1.6)
A [auth D]	UNK_F_TYPE	e4rpnD2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: UNK_F_TYPE	ECOD (1.6)
C [auth A]	LysR_substrate_2	e4rpnA2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: LysR_substrate_2	ECOD (1.6)
C [auth A]	UNK_F_TYPE	e4rpnA1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: UNK_F_TYPE	ECOD (1.6)
D [auth B]	LysR_substrate_2	e4rpnB1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: LysR_substrate_2	ECOD (1.6)
D [auth B]	UNK_F_TYPE	e4rpnB2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: UNK_F_TYPE	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth C]	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
A [auth D]	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
C [auth A]	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
D [auth B]	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth D], B [auth C], C [auth A], D [auth B]	PF03466	LysR substrate binding domain (LysR_substrate)	LysR substrate binding domain	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth D], B [auth C], C [auth A], D [auth B]	PCP degradation transcriptional activation protein	DNA binding binding organic cyclic compound binding nucleic acid binding transcription regulator activity DNA-binding transcription factor activity	catabolic process metabolic process cellular process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth D], B [auth C], C [auth A], D [auth B]	IPR005119	LysR, substrate-binding	Domain
A [auth D], B [auth C], C [auth A], D [auth B]	IPR036388	Winged helix-like DNA-binding domain superfamily	Homologous Superfamily
A [auth D], B [auth C], C [auth A], D [auth B]	IPR050389	LysR-type Transcriptional Regulators	Family
A [auth D], B [auth C], C [auth A], D [auth B]	IPR036390	Winged helix DNA-binding domain superfamily	Homologous Superfamily
A [auth D], B [auth C], C [auth A], D [auth B]	IPR000847	Transcription regulator HTH, LysR	Domain

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.