1XQ6

X-ray Structure of Gene Product from Arabidopsis Thaliana At5g02240

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)
B	d1xq6b1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Hypothetical protein At5g02240 (T7H20_290)	thale cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
B	d1xq6b2	Artifacts	Tags	Tags	Tags	N-terminal Tags	thale cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
A	d1xq6a1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Hypothetical protein At5g02240 (T7H20_290)	thale cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
A	d1xq6a2	Artifacts	Tags	Tags	Tags	N-terminal Tags	thale cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	SDR-like	8057139	3000038	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	SDR-like	8057139	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)
B	NAD_binding_10	e1xq6B1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: NAD_binding_10	ECOD (1.6)
A	NAD_binding_10	e1xq6A1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: NAD_binding_10	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
A	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	PF13460	NAD(P)H-binding (NAD_binding_10)	NAD(P)H-binding	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	unknown protein	oxidoreductase activity catalytic activity	response to abscisic acid response to stimulus response to lipid response to hormone response to alcohol response to chemical response to endogenous stimulus response to oxygen-containing compound	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol cell periphery plasma membrane membrane extracellular region apoplast membrane-bounded organelle plastid intracellular membrane-bounded organelle intracellular organelle plastid stroma intracellular anatomical structure cytoplasm cellular anatomical entity cytosol cell periphery plasma membrane membrane extracellular region apoplast membrane-bounded organelle plastid intracellular membrane-bounded organelle intracellular organelle plastid stroma organelle chloroplast stroma chloroplast plant-type vacuole vacuole

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B	IPR044163	Sanguinarine reductase SARED1-like	Family
A, B	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.