1B9L | pdb_00001b9l

7,8-DIHYDRONEOPTERIN TRIPHOSPHATE EPIMERASE

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	d1b9la_	Alpha and beta proteins (a+b)	T-fold	Tetrahydrobiopterin biosynthesis enzymes-like	DHN aldolase/epimerase	7,8-dihydroneopterin triphosphate epimerase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1b9lb_	Alpha and beta proteins (a+b)	T-fold	Tetrahydrobiopterin biosynthesis enzymes-like	DHN aldolase/epimerase	7,8-dihydroneopterin triphosphate epimerase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1b9lc_	Alpha and beta proteins (a+b)	T-fold	Tetrahydrobiopterin biosynthesis enzymes-like	DHN aldolase/epimerase	7,8-dihydroneopterin triphosphate epimerase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
E	d1b9le_	Alpha and beta proteins (a+b)	T-fold	Tetrahydrobiopterin biosynthesis enzymes-like	DHN aldolase/epimerase	7,8-dihydroneopterin triphosphate epimerase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
F	d1b9lf_	Alpha and beta proteins (a+b)	T-fold	Tetrahydrobiopterin biosynthesis enzymes-like	DHN aldolase/epimerase	7,8-dihydroneopterin triphosphate epimerase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
G	d1b9lg_	Alpha and beta proteins (a+b)	T-fold	Tetrahydrobiopterin biosynthesis enzymes-like	DHN aldolase/epimerase	7,8-dihydroneopterin triphosphate epimerase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
H	d1b9lh_	Alpha and beta proteins (a+b)	T-fold	Tetrahydrobiopterin biosynthesis enzymes-like	DHN aldolase/epimerase	7,8-dihydroneopterin triphosphate epimerase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d1b9ld_	Alpha and beta proteins (a+b)	T-fold	Tetrahydrobiopterin biosynthesis enzymes-like	DHN aldolase/epimerase	7,8-dihydroneopterin triphosphate epimerase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	DHN aldolase/epimerase	8023471	4001721	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8035851	3000283	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8035851	3000283	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8035851	3000283	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8035851	3000283	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8035851	3000283	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8035851	3000283	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8035851	3000283	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8035851	3000283	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	FolB	e1b9lA1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: FolB	ECOD (1.6)
B	FolB	e1b9lB1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: FolB	ECOD (1.6)
C	FolB	e1b9lC1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: FolB	ECOD (1.6)
E	FolB	e1b9lE1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: FolB	ECOD (1.6)
F	FolB	e1b9lF1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: FolB	ECOD (1.6)
G	FolB	e1b9lG1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: FolB	ECOD (1.6)
H	FolB	e1b9lH1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: FolB	ECOD (1.6)
D	FolB	e1b9lD1	A: a+b two layers	X: T-fold	H: Tetrahydrobiopterin biosynthesis enzymes-like (From Topology)	T: Tetrahydrobiopterin biosynthesis enzymes-like	F: FolB	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1130.10	Alpha Beta	2-Layer Sandwich	GTP Cyclohydrolase I, domain 2	GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain	CATH (4.3.0)
B	3.30.1130.10	Alpha Beta	2-Layer Sandwich	GTP Cyclohydrolase I, domain 2	GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain	CATH (4.3.0)
C	3.30.1130.10	Alpha Beta	2-Layer Sandwich	GTP Cyclohydrolase I, domain 2	GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain	CATH (4.3.0)
E	3.30.1130.10	Alpha Beta	2-Layer Sandwich	GTP Cyclohydrolase I, domain 2	GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain	CATH (4.3.0)
F	3.30.1130.10	Alpha Beta	2-Layer Sandwich	GTP Cyclohydrolase I, domain 2	GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain	CATH (4.3.0)
G	3.30.1130.10	Alpha Beta	2-Layer Sandwich	GTP Cyclohydrolase I, domain 2	GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain	CATH (4.3.0)
H	3.30.1130.10	Alpha Beta	2-Layer Sandwich	GTP Cyclohydrolase I, domain 2	GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal domain	CATH (4.3.0)
D	3.30.1130.10	Alpha Beta	2-Layer Sandwich	GTP Cyclohydrolase I, domain 2	GTP cyclohydrolase I, C-terminal domain/NADPH-dependent 7-cyano-7-deazaguanine reductase, N-terminal 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	PF02152	Dihydroneopterin aldolase (FolB)	Dihydroneopterin aldolase	This enzyme EC:4.1.2.25 catalyses the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin in the biosynthetic pathway of tetrahydrofolate.	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	PROTEIN (EPIMERASE)	isomerase activity racemase and epimerase activity dihydroneopterin triphosphate 2'-epimerase activity catalytic activity dihydroneopterin aldolase activity lyase activity carbon-carbon lyase activity aldehyde-lyase activity identical protein binding protein binding binding	folic acid-containing compound metabolic process modified amino acid metabolic process metabolic process cellular process pteridine-containing compound metabolic process biosynthetic process pteridine-containing compound biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm 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	IPR006156	Dihydroneopterin aldolase	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR006157	Dihydroneopterin aldolase/epimerase domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR043133	GTP cyclohydrolase I, C-terminal/NADPH-dependent 7-cyano-7-deazaguanine reductase	Homologous Superfamily

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.