3L49

CRYSTAL STRUCTURE OF ABC SUGAR TRANSPORTER SUBUNIT FROM Rhodobacter sphaeroides 2.4.1

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	d3l49a1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like I	Periplasmic binding protein-like I	automated matches	automated matches	(Cereibacter sphaeroides 2.4.1 ) [TaxId: 272943 ],	SCOPe (2.08)
A	d3l49a2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Cereibacter sphaeroides 2.4.1 ) [TaxId: 272943 ],	SCOPe (2.08)
B	d3l49b1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like I	Periplasmic binding protein-like I	automated matches	automated matches	(Cereibacter sphaeroides 2.4.1 ) [TaxId: 272943 ],	SCOPe (2.08)
B	d3l49b2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Cereibacter sphaeroides 2.4.1 ) [TaxId: 272943 ],	SCOPe (2.08)
C	d3l49c1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like I	Periplasmic binding protein-like I	automated matches	automated matches	(Cereibacter sphaeroides 2.4.1 ) [TaxId: 272943 ],	SCOPe (2.08)
C	d3l49c2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Cereibacter sphaeroides 2.4.1 ) [TaxId: 272943 ],	SCOPe (2.08)
D	d3l49d1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like I	Periplasmic binding protein-like I	automated matches	automated matches	(Cereibacter sphaeroides 2.4.1 ) [TaxId: 272943 ],	SCOPe (2.08)
D	d3l49d2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Cereibacter sphaeroides 2.4.1 ) [TaxId: 272943 ],	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	PF13407	e3l49A1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Periplasmic binding protein-like I	F: PF13407	ECOD (1.6)
B	PF13407	e3l49B3	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Periplasmic binding protein-like I	F: PF13407	ECOD (1.6)
C	PF13407	e3l49C3	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Periplasmic binding protein-like I	F: PF13407	ECOD (1.6)
D	PF13407	e3l49D1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Periplasmic binding protein-like I	F: PF13407	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.2300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Response regulator	CATH (4.3.0)
B	3.40.50.2300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Response regulator	CATH (4.3.0)
C	3.40.50.2300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Response regulator	CATH (4.3.0)
D	3.40.50.2300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Response regulator	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF13407	Periplasmic binding protein domain (Peripla_BP_4)	Periplasmic binding protein domain	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	ABC sugar (Ribose) transporter, periplasmic substrate-binding subunit	binding carbohydrate binding	-	periplasmic space cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR025997	Periplasmic binding protein	Domain
A, B, C, D	IPR028082	Periplasmic binding protein-like I	Homologous Superfamily

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.