1POY

SPERMIDINE/PUTRESCINE-BINDING PROTEIN COMPLEXED WITH SPERMIDINE (DIMER FORM)

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 [auth 1]	d1poy1_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Spermidine/putrescine-binding protein PotD	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B [auth 2]	d1poy2_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Spermidine/putrescine-binding protein PotD	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C [auth 3]	d1poy3_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Spermidine/putrescine-binding protein PotD	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D [auth 4]	d1poy4_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Spermidine/putrescine-binding protein PotD	(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)
A [auth 1]	SCOP2B Superfamily	Type 2 solute binding protein-like	8033350	3000083	SCOP2B (2022-06-29)
B [auth 2]	SCOP2B Superfamily	Type 2 solute binding protein-like	8033350	3000083	SCOP2B (2022-06-29)
C [auth 3]	SCOP2B Superfamily	Type 2 solute binding protein-like	8033350	3000083	SCOP2B (2022-06-29)
D [auth 4]	SCOP2B Superfamily	Type 2 solute binding protein-like	8033350	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)
A [auth 1]	SBP_bac_6_1	e1poy12	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: SBP_bac_6_1	ECOD (1.6)
A [auth 1]	SBP_bac_1_N_1	e1poy11	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: SBP_bac_1_N_1	ECOD (1.6)
B [auth 2]	SBP_bac_6_1	e1poy21	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: SBP_bac_6_1	ECOD (1.6)
B [auth 2]	SBP_bac_1_N_1	e1poy22	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: SBP_bac_1_N_1	ECOD (1.6)
C [auth 3]	SBP_bac_6_1	e1poy32	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: SBP_bac_6_1	ECOD (1.6)
C [auth 3]	SBP_bac_1_N_1	e1poy31	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: SBP_bac_1_N_1	ECOD (1.6)
D [auth 4]	SBP_bac_6_1	e1poy42	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: SBP_bac_6_1	ECOD (1.6)
D [auth 4]	SBP_bac_1_N_1	e1poy41	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: SBP_bac_1_N_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth 1]	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
B [auth 2]	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
C [auth 3]	3.40.190.10	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
D [auth 4]	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 1], B [auth 2], C [auth 3], D [auth 4]	PF13416	Bacterial extracellular solute-binding protein (SBP_bac_8)	Bacterial extracellular solute-binding protein	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth 1], B [auth 2], C [auth 3], D [auth 4]	SPERMIDINE/PUTRESCINE-BINDING PROTEIN	cation binding polyamine binding binding ion binding amine binding putrescine binding small molecule binding spermidine binding	localization nitrogen compound transport putrescine transport transport organic substance transport establishment of localization polyamine transport organic cation transport spermidine transport spermidine transmembrane transport transmembrane transport polyamine transmembrane transport cellular process	membrane cellular anatomical entity outer membrane-bounded periplasmic space cell envelope periplasmic space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth 1], B [auth 2], C [auth 3], D [auth 4]	IPR006059	Bacterial-type extracellular solute-binding protein	Family
A [auth 1], B [auth 2], C [auth 3], D [auth 4]	IPR001188	Spermidine/putrescine-binding periplasmic protein	Family

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.