4MCO

Crystal structure of a TRAP periplasmic solute binding protein from Rhodoferax ferrireducens (Rfer_1840), target EFI-510211, with bound malonate

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	d4mcoa1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	TRAP dicarboxylate transporter	(Rhodoferax ferrireducens T118 ) [TaxId: 338969 ],	SCOPe (2.08)
A	d4mcoa2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Rhodoferax ferrireducens T118 ) [TaxId: 338969 ],	SCOPe (2.08)
B	d4mcob1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	TRAP dicarboxylate transporter	(Rhodoferax ferrireducens T118 ) [TaxId: 338969 ],	SCOPe (2.08)
B	d4mcob2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Rhodoferax ferrireducens T118 ) [TaxId: 338969 ],	SCOPe (2.08)
C	d4mcoc1	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	TRAP dicarboxylate transporter	(Rhodoferax ferrireducens T118 ) [TaxId: 338969 ],	SCOPe (2.08)
C	d4mcoc2	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Rhodoferax ferrireducens T118 ) [TaxId: 338969 ],	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	DctP	e4mcoA1	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: DctP	ECOD (1.6)
B	DctP	e4mcoB1	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: DctP	ECOD (1.6)
C	DctP	e4mcoC1	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: DctP	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.190.170	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
B	3.40.190.170	Alpha Beta	3-Layer(aba) Sandwich	D-Maltodextrin-Binding Protein	domain 2	CATH (4.3.0)
C	3.40.190.170	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, B, C	PF03480	Bacterial extracellular solute-binding protein, family 7 (DctP)	Bacterial extracellular solute-binding protein, family 7	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	TRAP dicarboxylate transporter-DctP subunit	-	organic acid transport localization organic anion transport carboxylic acid transport transport dicarboxylic acid transport C4-dicarboxylate transport establishment of localization transmembrane transport cellular process	cellular anatomical structure periplasmic space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR018389	TRAP transporter solute receptor DctP	Family
A, B, C	IPR038404	TRAP transporter solute receptor DctP superfamily	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.