2QP4 | pdb_00002qp4

Identification and Characterization of Two Amino Acids Critical for the Substrate Inhibition of SULT2A1

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
Pharos: Disease Associations

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2qp4a_	Alpha and beta proteins (a/b)	P-loop containing nucleoside triphosphate hydrolases	P-loop containing nucleoside triphosphate hydrolases	PAPS sulfotransferase	Hydroxysteroid sulfotransferase sult2a1	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	P-loop nucleotide/nucleoside kinase-like	8057104	3002021	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	Sulfotransfer_1	e2qp4A1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: Sulfotransfer_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.300	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	P-loop containing nucleotide triphosphate hydrolases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00685	Sulfotransferase domain (Sulfotransfer_1)	Sulfotransferase domain		Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Bile salt sulfotransferase	3'-phosphoadenosine 5'-phosphosulfate binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding 3'-phosphoadenosine 5'-phosphosulfate binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding sulfur compound binding transferase activity, transferring sulphur-containing groups sulfotransferase activity transferase activity catalytic activity bile-salt sulfotransferase activity steroid sulfotransferase activity alcohol sulfotransferase activity	lipid catabolic process catabolic process metabolic process cellular process primary metabolic process lipid metabolic process steroid metabolic process cellular response to stimulus cellular response to chemical stimulus response to stimulus response to chemical cellular response to xenobiotic stimulus xenobiotic metabolic process response to xenobiotic stimulus lipid catabolic process catabolic process metabolic process cellular process primary metabolic process lipid metabolic process steroid metabolic process cellular response to stimulus cellular response to chemical stimulus response to stimulus response to chemical cellular response to xenobiotic stimulus xenobiotic metabolic process response to xenobiotic stimulus sulfur compound metabolic process sulfation ribose phosphate metabolic process nucleoside bisphosphate metabolic process purine nucleoside bisphosphate metabolic process ribonucleoside bisphosphate metabolic process oxoacid metabolic process carbohydrate derivative metabolic process organic acid metabolic process purine ribonucleoside bisphosphate metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process small molecule metabolic process phosphorus metabolic process nucleoside phosphate metabolic process 3'-phosphoadenosine 5'-phosphosulfate metabolic process nucleotide metabolic process purine-containing compound metabolic process organophosphate metabolic process purine ribonucleotide metabolic process regulation of hormone levels phenol-containing compound metabolic process biological regulation modified amino acid metabolic process regulation of biological quality hormone metabolic process thyroid hormone metabolic process carboxylic acid metabolic process organic acid catabolic process bile acid catabolic process bile acid metabolic process monocarboxylic acid catabolic process carboxylic acid catabolic process monocarboxylic acid metabolic process small molecule catabolic process secondary alcohol metabolic process sterol metabolic process cholesterol metabolic process alcohol metabolic process alcohol catabolic process primary alcohol catabolic process ethanol metabolic process ethanol catabolic process primary alcohol metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR000863	Sulfotransferase domain	Domain
A	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A	Pharos: Q06520	Liver Cirrhosis, Experimental prostate cancer gallbladder disease gastric carcinoma pancreatic ductal adenocarcinoma interstitial cystitis

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.