3H4V

Selective screening and design to identify inhibitors of leishmania major pteridine reductase 1

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3h4va_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Dihydropteridin reductase (pteridine reductase)	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)
B	d3h4vb_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Dihydropteridin reductase (pteridine reductase)	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)
C	d3h4vc_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Dihydropteridin reductase (pteridine reductase)	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)
D	d3h4vd_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Dihydropteridin reductase (pteridine reductase)	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)
E	d3h4ve_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Dihydropteridin reductase (pteridine reductase)	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)
F	d3h4vf_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Dihydropteridin reductase (pteridine reductase)	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)
G	d3h4vg_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Dihydropteridin reductase (pteridine reductase)	(Leishmania major ) [TaxId: 5664 ],	SCOPe (2.08)
H	d3h4vh_	Alpha and beta proteins (a/b)	NAD(P)-binding Rossmann-fold domains	NAD(P)-binding Rossmann-fold domains	Tyrosine-dependent oxidoreductases	Dihydropteridin reductase (pteridine reductase)	(Leishmania major ) [TaxId: 5664 ],	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	8057127	3000038	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	SDR-like	8057127	3000038	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	SDR-like	8057127	3000038	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	SDR-like	8057127	3000038	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	SDR-like	8057127	3000038	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	SDR-like	8057127	3000038	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	SDR-like	8057127	3000038	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	SDR-like	8057127	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	e3h4vA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
B	adh_short_C2	e3h4vB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
C	adh_short_C2	e3h4vC1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
D	adh_short_C2	e3h4vD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
E	adh_short_C2	e3h4vE1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
F	adh_short_C2	e3h4vF1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
G	adh_short_C2	e3h4vG1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	ECOD (1.6)
H	adh_short_C2	e3h4vH1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: adh_short_C2	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)
E	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	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)
G	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)
H	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, E A, B, C, D, E, F, G, H	PF13561	Enoyl-(Acyl carrier protein) reductase (adh_short_C2)	Enoyl-(Acyl carrier protein) reductase	This domain is found in Enoyl-(Acyl carrier protein) reductases.	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, G, H	Pteridine reductase 1	oxidoreductase activity catalytic activity oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on the CH-NH group of donors 6,7-dihydropteridine reductase activity pteridine reductase activity	polyol metabolic process small molecule biosynthetic process organic hydroxy compound metabolic process alcohol metabolic process diol biosynthetic process diol metabolic process biosynthetic process tetrahydrobiopterin biosynthetic process tetrahydrobiopterin metabolic process organic hydroxy compound biosynthetic process pteridine-containing compound biosynthetic process polyol biosynthetic process alcohol biosynthetic process metabolic process polyol metabolic process small molecule biosynthetic process organic hydroxy compound metabolic process alcohol metabolic process diol biosynthetic process diol metabolic process biosynthetic process tetrahydrobiopterin biosynthetic process tetrahydrobiopterin metabolic process organic hydroxy compound biosynthetic process pteridine-containing compound biosynthetic process polyol biosynthetic process alcohol biosynthetic process metabolic process small molecule metabolic process pteridine-containing compound metabolic process response to methotrexate response to stimulus response to chemical response to oxygen-containing compound response to nitrogen compound response to organic cyclic compound	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR002347	Short-chain dehydrogenase/reductase SDR	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR014058	Pteridine reductase	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR020904	Short-chain dehydrogenase/reductase, conserved site	Conserved Site

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.