5LLN

Crystal structure of human carbonic anhydrase isozyme XIII with 2,3,5,6-Tetrafluoro-4-(propylthio)benzenesulfonamide

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 [auth B]	d5llnb_	All beta proteins	Carbonic anhydrase	Carbonic anhydrase	Carbonic anhydrase	automated matches	Human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B [auth A]	d5llna_	All beta proteins	Carbonic anhydrase	Carbonic anhydrase	Carbonic anhydrase	automated matches	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 [auth B]	SCOP2B Superfamily	Carbonic anhydrase	8065111	3001672	SCOP2B (2022-06-29)
B [auth A]	SCOP2B Superfamily	Carbonic anhydrase	8065111	3001672	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 [auth B]	Carb_anhydrase	e5llnB1	A: beta meanders	X: Carbonic anhydrase (From Topology)	H: Carbonic anhydrase (From Topology)	T: Carbonic anhydrase	F: Carb_anhydrase	ECOD (1.6)
B [auth A]	Carb_anhydrase	e5llnA1	A: beta meanders	X: Carbonic anhydrase (From Topology)	H: Carbonic anhydrase (From Topology)	T: Carbonic anhydrase	F: Carb_anhydrase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth B]	3.10.200.10	Alpha Beta	Roll	Carbonic Anhydrase II	Alpha carbonic anhydrase	CATH (4.3.0)
B [auth A]	3.10.200.10	Alpha Beta	Roll	Carbonic Anhydrase II	Alpha carbonic anhydrase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth A]	PF00194	Eukaryotic-type carbonic anhydrase (Carb_anhydrase)	Eukaryotic-type carbonic anhydrase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth A]	Carbonic anhydrase 13	cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding carbonate dehydratase activity hydro-lyase activity lyase activity catalytic activity carbon-oxygen lyase activity	cellular metabolic process small molecule metabolic process metabolic process cellular process one-carbon metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane-bounded organelle intracellular organelle organelle intracellular membrane-bounded organelle myelin sheath

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth A]	IPR018338	Carbonic anhydrase, alpha-class, conserved site	Conserved Site
A [auth B], B [auth A]	IPR001148	Alpha carbonic anhydrase domain	Domain
A [auth B], B [auth A]	IPR036398	Alpha carbonic anhydrase domain superfamily	Homologous Superfamily
A [auth B], B [auth A]	IPR023561	Carbonic anhydrase, alpha-class	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A [auth B], B [auth A]	Pharos: Q8N1Q1	atopic eczema Crohn disease malignant pancreatic neoplasm pancreatic intraductal papillary-mucinous neoplasm tuberculosis atypical teratoid rhabdoid tumor cystic fibrosis medulloblastoma psoriasis ulcerative colitis breast cancer large cell medulloblastoma ovarian cancer transitional cell carcinoma

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.