4C49

Reactive loop cleaved human CBG in complex with cortisol

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	d4c49a_	Multi-domain proteins (alpha and beta)	Serpins	Serpins	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d4c49c_	Multi-domain proteins (alpha and beta)	Serpins	Serpins	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d4c49d_	Multi-domain proteins (alpha and beta)	Serpins	Serpins	automated matches	automated matches	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d4c49b_	Multi-domain proteins (alpha and beta)	Serpins	Serpins	automated matches	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	SCOP2B Superfamily	Serpins	8070153	3001563	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Serpins	8070153	3001563	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Serpins	8070153	3001563	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Serpins	8070153	3001563	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	Serpin	e4c49A1	A: a+b complex topology	X: Serpins (From Topology)	H: Serpins (From Topology)	T: Serpins	F: Serpin	ECOD (1.6)
C	Serpin	e4c49C1	A: a+b complex topology	X: Serpins (From Topology)	H: Serpins (From Topology)	T: Serpins	F: Serpin	ECOD (1.6)
D	Serpin	e4c49D1	A: a+b complex topology	X: Serpins (From Topology)	H: Serpins (From Topology)	T: Serpins	F: Serpin	ECOD (1.6)
B	Serpin	e4c49B1	A: a+b complex topology	X: Serpins (From Topology)	H: Serpins (From Topology)	T: Serpins	F: Serpin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.497.10	Alpha Beta	2-Layer Sandwich	Antithrombin	Chain I, domain 2	CATH (4.3.0)
A	2.30.39.10	Mainly Beta	Roll	Alpha-1-antitrypsin	domain 1	CATH (4.3.0)
C	3.30.497.10	Alpha Beta	2-Layer Sandwich	Antithrombin	Chain I, domain 2	CATH (4.3.0)
C	2.30.39.10	Mainly Beta	Roll	Alpha-1-antitrypsin	domain 1	CATH (4.3.0)
D	3.30.497.10	Alpha Beta	2-Layer Sandwich	Antithrombin	Chain I, domain 2	CATH (4.3.0)
D	2.30.39.10	Mainly Beta	Roll	Alpha-1-antitrypsin	domain 1	CATH (4.3.0)
B	3.30.497.10	Alpha Beta	2-Layer Sandwich	Antithrombin	Chain I, domain 2	CATH (4.3.0)
B	2.30.39.10	Mainly Beta	Roll	Alpha-1-antitrypsin	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00079	Serpin (serine protease inhibitor) (Serpin)	Serpin (serine protease inhibitor)	Structure is a multi-domain fold containing a bundle of helices and a beta sandwich.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	CORTICOSTEROID-BINDING GLOBULIN	enzyme regulator activity molecular function inhibitor activity peptidase regulator activity serine-type endopeptidase inhibitor activity molecular function regulator activity enzyme inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity binding organic cyclic compound binding steroid binding lipid binding	glucocorticoid metabolic process steroid metabolic process primary metabolic process metabolic process cellular process lipid metabolic process	cellular anatomical structure extracellular region extracellular space extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle organelle vesicle extracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR042178	Serpin superfamily, domain 1	Homologous Superfamily
A, B, C, D	IPR023795	Serpin, conserved site	Conserved Site
A, B, C, D	IPR042185	Serpin superfamily, domain 2	Homologous Superfamily
A, B, C, D	IPR036186	Serpin superfamily	Homologous Superfamily
A, B, C, D	IPR000215	Serpin family	Family
A, B, C, D	IPR023796	Serpin domain	Domain

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: P08185	corticosteroid-binding globulin deficiency autoimmune disease cirrhosis of liver Liver Cirrhosis, Experimental hemorrhoid ulcerative colitis miliary tuberculosis dermatitis herpetiformis bacterial conjunctivitis musculoskeletal system disease Diamond-Blackfan anemia rosacea seborrheic dermatitis hypopituitarism pancreatic ductal adenocarcinoma corticosteroid-binding globulin deficiency autoimmune disease cirrhosis of liver Liver Cirrhosis, Experimental hemorrhoid ulcerative colitis miliary tuberculosis dermatitis herpetiformis bacterial conjunctivitis musculoskeletal system disease Diamond-Blackfan anemia rosacea seborrheic dermatitis hypopituitarism pancreatic ductal adenocarcinoma skin disease pemphigus Addison disease Stevens-Johnson syndrome inherited aplastic anemia polymyalgia rheumatica epicondylitis allergic bronchopulmonary aspergillosis synovitis iritis contact dermatitis postmenopausal osteoporosis systemic lupus erythematosus keratitis corneal ulcer extrinsic allergic alveolitis ankylosing spondylitis tenosynovitis fatty liver disease gallbladder disease asthma tinea pedis psoriasis granuloma annulare pulmonary fibrosis autoimmune hemolytic anemia uveitis dermatophytosis of groin and perianal area rheumatic heart disease mycosis fungoides sarcoidosis blepharoconjunctivitis drug-induced liver injury idiopathic acute eosinophilic pneumonia cerebrovascular disorder pancreatic intraductal papillary-mucinous carcinoma endogenous depression acquired thrombocytopenia inflammatory bowel disease endometriosis adrenocortical insufficiency erythema multiforme allergic rhinitis temporal arteritis Klinefelter syndrome eye disease aphthous stomatitis thyroiditis Crohn disease atopic conjunctivitis dacryocystitis psoriatic arthritis heart disease autism spectrum disorder trichinosis depressive disorder autoimmune thrombocytopenic purpura multiple sclerosis rheumatoid arthritis Hodgkins lymphoma nephrotic syndrome hypogonadotropic hypogonadism bursitis otitis externa Sjogren syndrome pancreatic intraductal papillary-mucinous neoplasm with low grade dysplasia endometrial carcinoma acute lymphoblastic leukemia chronic beryllium disease pneumocystosis eosinophilic pneumonia alcoholic liver cirrhosis sympathetic ophthalmia iridocyclitis congenital adrenal hyperplasia juvenile idiopathic arthritis primary cutaneous T-cell lymphoma exanthem angioedema tendinitis proctitis aspiration pneumonitis tinea corporis cryptorchidism gout atopic eczema pulmonary eosinophilia

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.