3DEL

The structure of CT381, the arginine binding protein from the periplasm Chlamydia trachomatis

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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 [auth B]	d3delb1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Chlamydia trachomatis ) [TaxId: 813 ],	SCOPe (2.08)
A [auth B]	d3delb2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Chlamydia trachomatis ) [TaxId: 813 ],	SCOPe (2.08)
B [auth C]	d3delc1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Chlamydia trachomatis ) [TaxId: 813 ],	SCOPe (2.08)
B [auth C]	d3delc2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Chlamydia trachomatis ) [TaxId: 813 ],	SCOPe (2.08)
C [auth D]	d3deld1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Chlamydia trachomatis ) [TaxId: 813 ],	SCOPe (2.08)
C [auth D]	d3deld2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Chlamydia trachomatis ) [TaxId: 813 ],	SCOPe (2.08)
D [auth F]	d3delf1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	automated matches	automated matches	(Chlamydia trachomatis ) [TaxId: 813 ],	SCOPe (2.08)
D [auth F]	d3delf2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Chlamydia trachomatis ) [TaxId: 813 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth B]	F_UNCLASSIFIED	e3delB1	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: F_UNCLASSIFIED	ECOD (1.6)
A [auth B]	PF00497	e3delB2	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: PF00497	ECOD (1.6)
B [auth C]	F_UNCLASSIFIED	e3delC1	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: F_UNCLASSIFIED	ECOD (1.6)
B [auth C]	PF00497	e3delC2	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: PF00497	ECOD (1.6)
C [auth D]	F_UNCLASSIFIED	e3delD2	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: F_UNCLASSIFIED	ECOD (1.6)
C [auth D]	PF00497	e3delD1	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: PF00497	ECOD (1.6)
D [auth F]	F_UNCLASSIFIED	e3delF1	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: F_UNCLASSIFIED	ECOD (1.6)
D [auth F]	PF00497	e3delF2	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: PF00497	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth B]	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
B [auth C]	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
C [auth D]	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
D [auth F]	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 B], B [auth C], C [auth D], D [auth F]	PF00497	Bacterial extracellular solute-binding proteins, family 3 (SBP_bac_3)	Bacterial extracellular solute-binding proteins, family 3	This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. Th ...	This is a sensor domain found in solute-binding protein family 3 members from Gram-positive bacteria, Gram-negative bacteria and archaea. It can also be found in the N-terminal of the membrane-bound lytic murein transglycosylase F (MltF) protein. This domain recognises Nicotinate, quidalnate, pyridine-2,5-dicarboxylate and salicylate [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth C], C [auth D], D [auth F]	Arginine Binding Protein	-	amino acid transport localization transport organic substance transport establishment of localization	cell surface cellular anatomical entity extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth C], C [auth D], D [auth F]	IPR037297	Probable ABC transporter arginine-binding protein ArtJ, PBP2 domain	Domain
A [auth B], B [auth C], C [auth D], D [auth F]	IPR001638	Solute-binding protein family 3/N-terminal domain of MltF	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.