1FDU

HUMAN 17-BETA-HYDROXYSTEROID-DEHYDROGENASE TYPE 1 MUTANT H221L COMPLEXED WITH ESTRADIOL AND NADP+

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	d1fdua_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Human estrogenic 17beta-hydroxysteroid dehydrogenase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1fdub_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Human estrogenic 17beta-hydroxysteroid dehydrogenase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1fduc_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Human estrogenic 17beta-hydroxysteroid dehydrogenase	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d1fdud_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Human estrogenic 17beta-hydroxysteroid dehydrogenase	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	SDR-like	8044635	3000038	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	SDR-like	8044635	3000038	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	SDR-like	8044635	3000038	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	SDR-like	8044635	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	adh_short_C2_1	e1fduA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)
B	adh_short_C2_1	e1fduB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)
C	adh_short_C2_1	e1fduC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	ECOD (1.6)
D	adh_short_C2_1	e1fduD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2_1	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	PF00106	short chain dehydrogenase (adh_short)	short chain dehydrogenase	This family contains a wide variety of dehydrogenases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	17-BETA-HYDROXYSTEROID DEHYDROGENASE	steroid dehydrogenase activity oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors testosterone dehydrogenase [NAD(P)+] activity steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor testosterone dehydrogenase (NAD+) activity catalytic activity testosterone 17-beta-dehydrogenase (NADP+) activity binding organic cyclic compound binding estradiol binding steroid binding lipid binding steroid dehydrogenase activity oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors testosterone dehydrogenase [NAD(P)+] activity steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor testosterone dehydrogenase (NAD+) activity catalytic activity testosterone 17-beta-dehydrogenase (NADP+) activity binding organic cyclic compound binding estradiol binding steroid binding lipid binding NADP+ binding nucleotide binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding heterocyclic compound binding NADP binding small molecule binding identical protein binding protein binding protein homodimerization activity protein dimerization activity estradiol 17-beta-dehydrogenase [NAD(P)+] activity 17-beta-hydroxysteroid dehydrogenase (NADP+) activity	developmental process connective tissue development adipose tissue development animal organ development anatomical structure development tissue development olefinic compound biosynthetic process small molecule biosynthetic process cellular biosynthetic process organic hydroxy compound metabolic process cellular metabolic process steroid metabolic process lipid biosynthetic process primary metabolic process developmental process connective tissue development adipose tissue development animal organ development anatomical structure development tissue development olefinic compound biosynthetic process small molecule biosynthetic process cellular biosynthetic process organic hydroxy compound metabolic process cellular metabolic process steroid metabolic process lipid biosynthetic process primary metabolic process testosterone biosynthetic process cellular ketone metabolic process biosynthetic process organic hydroxy compound biosynthetic process metabolic process olefinic compound metabolic process small molecule metabolic process cellular process steroid biosynthetic process ketone biosynthetic process lipid metabolic process estrogen metabolic process regulation of hormone levels biological regulation regulation of biological quality hormone metabolic process multicellular organism development multicellular organismal process skeletal system development bone development system development cellular response to stimulus cellular response to metal ion cellular response to chemical stimulus response to stimulus response to metal ion response to chemical muscle structure development skeletal muscle organ development skeletal muscle tissue development muscle tissue development muscle organ development striated muscle tissue development cellular component organization lysosome organization organelle organization vacuole organization lytic vacuole organization cellular component organization or biogenesis macromolecule metabolic process gene expression macromolecule biosynthetic process estrogen biosynthetic process hormone biosynthetic process steroid hormone biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR011348	17beta-dehydrogenase	Family
A, B, C, D	IPR002347	Short-chain dehydrogenase/reductase SDR	Family
A, B, C, D	IPR020904	Short-chain dehydrogenase/reductase, conserved site	Conserved Site
A, B, C, D	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: P14061	endometriosis prostate cancer Abortion, Spontaneous metabolic syndrome X psoriasis non-small cell lung carcinoma cystic fibrosis lung adenocarcinoma

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.