1ORR

Crystal Structure of CDP-Tyvelose 2-Epimerase complexed with NAD and CDP

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	d1orra1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	CDP-tyvelose-2-epimerase	(Salmonella enterica subsp. enterica serovar Typhi ) [TaxId: 90370 ],	SCOPe (2.08)
A	d1orra2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Salmonella enterica subsp. enterica serovar Typhi ) [TaxId: 90370 ],	SCOPe (2.08)
B	d1orrb1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	CDP-tyvelose-2-epimerase	(Salmonella enterica subsp. enterica serovar Typhi ) [TaxId: 90370 ],	SCOPe (2.08)
B	d1orrb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Salmonella enterica subsp. enterica serovar Typhi ) [TaxId: 90370 ],	SCOPe (2.08)
C	d1orrc1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	CDP-tyvelose-2-epimerase	(Salmonella enterica subsp. enterica serovar Typhi ) [TaxId: 90370 ],	SCOPe (2.08)
C	d1orrc2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Salmonella enterica subsp. enterica serovar Typhi ) [TaxId: 90370 ],	SCOPe (2.08)
D	d1orrd1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	CDP-tyvelose-2-epimerase	(Salmonella enterica subsp. enterica serovar Typhi ) [TaxId: 90370 ],	SCOPe (2.08)
D	d1orrd2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Salmonella enterica subsp. enterica serovar Typhi ) [TaxId: 90370 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	UDP-glucose 4-epimerase GalE-lke	8058107	4000088	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	SDR-like	8058108	3000038	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	SDR-like	8058108	3000038	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	SDR-like	8058108	3000038	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	SDR-like	8058108	3000038	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	GDP_Man_Dehyd	e1orrA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: GDP_Man_Dehyd	ECOD (1.6)
B	GDP_Man_Dehyd	e1orrB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: GDP_Man_Dehyd	ECOD (1.6)
C	GDP_Man_Dehyd	e1orrC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: GDP_Man_Dehyd	ECOD (1.6)
D	GDP_Man_Dehyd	e1orrD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: GDP_Man_Dehyd	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
C	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
D	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF16363	GDP-mannose 4,6 dehydratase (GDP_Man_Dehyd)	GDP-mannose 4,6 dehydratase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	CDP-tyvelose-2-epimerase	isomerase activity racemase and epimerase activity CDP-abequose epimerase activity racemase and epimerase activity, acting on carbohydrates and derivatives catalytic activity	lipopolysaccharide biosynthetic process carbohydrate derivative biosynthetic process carbohydrate metabolic process polysaccharide biosynthetic process cellular biosynthetic process carbohydrate biosynthetic process cellular metabolic process liposaccharide metabolic process lipid biosynthetic process carbohydrate derivative metabolic process primary metabolic process macromolecule biosynthetic process lipopolysaccharide metabolic process polysaccharide metabolic process biosynthetic process lipopolysaccharide biosynthetic process carbohydrate derivative biosynthetic process carbohydrate metabolic process polysaccharide biosynthetic process cellular biosynthetic process carbohydrate biosynthetic process cellular metabolic process liposaccharide metabolic process lipid biosynthetic process carbohydrate derivative metabolic process primary metabolic process macromolecule biosynthetic process lipopolysaccharide metabolic process polysaccharide metabolic process biosynthetic process metabolic process cellular process macromolecule metabolic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B, C, D	IPR016040	NAD(P)-binding domain	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.