1ZBQ

Crystal Structure Of Human 17-Beta-Hydroxysteroid Dehydrogenase Type 4 In Complex With NAD

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	d1zbqa1	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Peroxisomal multifunctional enzyme type 2	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1zbqb_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Peroxisomal multifunctional enzyme type 2	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1zbqc_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Peroxisomal multifunctional enzyme type 2	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d1zbqd_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Peroxisomal multifunctional enzyme type 2	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d1zbqe_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Peroxisomal multifunctional enzyme type 2	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d1zbqf_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Peroxisomal multifunctional enzyme type 2	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	SCOP2 Family	Short-chain dehydrogenases/reductases, SDR	8017572	4000029	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	SDR-like	8057125	3000038	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	SDR-like	8057125	3000038	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	SDR-like	8057125	3000038	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	SDR-like	8057125	3000038	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	SDR-like	8057125	3000038	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	SDR-like	8057125	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	e1zbqA1	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	e1zbqB1	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	e1zbqC1	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	e1zbqD1	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)
E	adh_short_C2_1	e1zbqE1	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)
F	adh_short_C2_1	e1zbqF1	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)
A	1.10.287.4290	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		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)
B	1.10.287.4290	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		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)
C	1.10.287.4290	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		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)
D	1.10.287.4290	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
E	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
E	1.10.287.4290	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)
F	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
F	1.10.287.4290	Mainly Alpha	Orthogonal Bundle	Helix Hairpins		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	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, E A, B, C, D, E, F	17-beta-hydroxysteroid dehydrogenase 4	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 (3R)-hydroxyacyl-CoA dehydrogenase (NAD+) activity catalytic activity enoyl-CoA hydratase activity hydro-lyase activity 3-hydroxyacyl-CoA dehydratase activity lyase activity carbon-oxygen lyase activity 3-hydroxyacyl-CoA dehydrogenase activity steroid dehydrogenase activity steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor 17-beta-hydroxysteroid dehydrogenase (NAD+) 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 (3R)-hydroxyacyl-CoA dehydrogenase (NAD+) activity catalytic activity enoyl-CoA hydratase activity hydro-lyase activity 3-hydroxyacyl-CoA dehydratase activity lyase activity carbon-oxygen lyase activity 3-hydroxyacyl-CoA dehydrogenase activity steroid dehydrogenase activity steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor 17-beta-hydroxysteroid dehydrogenase (NAD+) activity 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA hydratase activity identical protein binding protein binding binding protein homodimerization activity protein dimerization activity isomerase activity estradiol 17-beta-dehydrogenase [NAD(P)+] activity	developmental process multicellular organismal process cellular developmental process ossification cell differentiation cellular process osteoblast differentiation nucleoside phosphate metabolic process very long-chain fatty-acyl-CoA metabolic process primary metabolic process purine-containing compound metabolic process fatty acid derivative metabolic process nucleobase-containing compound metabolic process acyl-CoA metabolic process developmental process multicellular organismal process cellular developmental process ossification cell differentiation cellular process osteoblast differentiation nucleoside phosphate metabolic process very long-chain fatty-acyl-CoA metabolic process primary metabolic process purine-containing compound metabolic process fatty acid derivative metabolic process nucleobase-containing compound metabolic process acyl-CoA metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process metabolic process sulfur compound metabolic process small molecule metabolic process fatty-acyl-CoA metabolic process amide metabolic process thioester metabolic process phosphorus metabolic process lipid metabolic process regulation of hormone levels steroid metabolic process biological regulation androgen metabolic process regulation of biological quality hormone metabolic process fatty acid metabolic process lipid catabolic process catabolic process oxoacid metabolic process carboxylic acid metabolic process lipid modification organic acid catabolic process organic acid metabolic process fatty acid catabolic process cellular catabolic process monocarboxylic acid catabolic process fatty acid oxidation carboxylic acid catabolic process fatty acid beta-oxidation monocarboxylic acid metabolic process lipid oxidation small molecule catabolic process estrogen metabolic process very long-chain fatty acid metabolic process reproductive process sex differentiation cell development developmental process involved in reproduction epithelial cell differentiation Sertoli cell differentiation male gonad development male sex differentiation multicellular organism development development of primary male sexual characteristics development of primary sexual characteristics anatomical structure development reproductive structure development system development epithelium development gonad development reproductive system development Sertoli cell development animal organ development tissue development epithelial cell development medium-chain fatty-acyl-CoA metabolic process	cellular anatomical structure membrane intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle organelle peroxisome microbody intracellular membrane-bounded organelle microbody membrane bounding membrane of organelle peroxisomal membrane cellular anatomical structure membrane intracellular anatomical structure cytoplasm cytosol membrane-bounded organelle intracellular organelle organelle peroxisome microbody intracellular membrane-bounded organelle microbody membrane bounding membrane of organelle peroxisomal membrane organelle membrane peroxisomal matrix membrane-enclosed lumen intracellular organelle lumen organelle lumen microbody lumen

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR051687	Peroxisomal Beta-Oxidation Enzymes	Family
A, B, C, D, E A, B, C, D, E, F	IPR002347	Short-chain dehydrogenase/reductase SDR	Family
A, B, C, D, E A, B, C, D, E, F	IPR020904	Short-chain dehydrogenase/reductase, conserved site	Conserved Site
A, B, C, D, E A, B, C, D, E, F	IPR036527	SCP2 sterol-binding domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR003033	SCP2 sterol-binding domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR029069	HotDog domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR002539	MaoC-like dehydratase domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR054357	Peroxisomal multifunctional enzyme type 2-like, N-terminal domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F	Pharos: P51659	d-bifunctional protein deficiency Perrault syndrome Zellweger spectrum disorders peroxisomal disease West syndrome Perrault syndrome 1 Peroxisomal Dysfunction, Single polycystic ovary syndrome Spasmus nutans developmental and epileptic encephalopathy lymphoplasmacytic lymphoma ovarian cancer allergic rhinitis leukodystrophy pancreatic ductal adenocarcinoma d-bifunctional protein deficiency Perrault syndrome Zellweger spectrum disorders peroxisomal disease West syndrome Perrault syndrome 1 Peroxisomal Dysfunction, Single polycystic ovary syndrome Spasmus nutans developmental and epileptic encephalopathy lymphoplasmacytic lymphoma ovarian cancer allergic rhinitis leukodystrophy pancreatic ductal adenocarcinoma tuberculosis dermatomyositis intellectual disability lung cancer

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.