7SU8

DIHYDRONEOPTERIN ALDOLASE (DHNA) FROM YERSINIA PESTIS with alkylated Cys50 CO-CRYSTALLIZED with 7,8-dihydroneopterin

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8101305	3000283	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Tetrahydrobiopterin biosynthesis enzymes-like	8101305	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	e7su8A1	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	e7su8B1	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	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	7,8-dihydroneopterin aldolase	dihydroneopterin aldolase activity lyase activity catalytic activity carbon-carbon lyase activity aldehyde-lyase activity	oxoacid metabolic process cellular biosynthetic process organonitrogen compound biosynthetic process vitamin biosynthetic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process small molecule metabolic process amide metabolic process water-soluble vitamin metabolic process folic acid metabolic process dicarboxylic acid biosynthetic process folic acid biosynthetic process folic acid-containing compound biosynthetic process oxoacid metabolic process cellular biosynthetic process organonitrogen compound biosynthetic process vitamin biosynthetic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process small molecule metabolic process amide metabolic process water-soluble vitamin metabolic process folic acid metabolic process dicarboxylic acid biosynthetic process folic acid biosynthetic process folic acid-containing compound biosynthetic process organonitrogen compound metabolic process water-soluble vitamin biosynthetic process small molecule biosynthetic process cellular metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process amide biosynthetic process cellular modified amino acid metabolic process vitamin metabolic process biosynthetic process cellular modified amino acid biosynthetic process folic acid-containing compound metabolic process pteridine-containing compound biosynthetic process metabolic process cellular process pteridine-containing compound metabolic process tetrahydrofolate biosynthetic process tetrahydrofolate metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR006156	Dihydroneopterin aldolase	Family
A, B	IPR006157	Dihydroneopterin aldolase/epimerase domain	Domain
A, B	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 R01GM133198.