1Q0N

CRYSTAL STRUCTURE OF A TERNARY COMPLEX OF 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN PYROPHOSPHOKINASE FROM E. COLI WITH MGAMPCPP AND 6-HYDROXYMETHYL-7,8-DIHYDROPTERIN AT 1.25 ANGSTROM RESOLUTION

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1q0na_	Alpha and beta proteins (a+b)	Ferredoxin-like	6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK	6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK	6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK	(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	SCOP2B Superfamily	6-hydroxymethyl-7, 8-dihydropterin pyrophosphokinase, HPPK	8044430	3001294	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	HPPK	e1q0nA1	A: a+b two layers	X: Alpha-beta plaits	H: 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK (From Topology)	T: 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK	F: HPPK	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.70.560	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF01288	7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK) (HPPK)	7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK)	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase	2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity diphosphotransferase activity transferase activity catalytic activity transferase activity, transferring phosphorus-containing groups cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity diphosphotransferase activity transferase activity catalytic activity transferase activity, transferring phosphorus-containing groups cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding kinase activity	oxoacid metabolic process modified amino acid 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 water-soluble vitamin biosynthetic process oxoacid metabolic process modified amino acid 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 water-soluble vitamin biosynthetic process small molecule biosynthetic process dicarboxylic acid metabolic process modified amino acid metabolic process carboxylic acid metabolic process amide biosynthetic process vitamin metabolic process 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	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR035907	7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK superfamily	Homologous Superfamily
A	IPR000550	7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase, HPPK	Domain

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase M-CSA #151	6-Hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) catalyses the transfer of pyrophosphate from ATP to 6-hydroxymethyl-7,8-dihydropterin(HP), the first reaction in the folate biosynthesis. Folate cofactors are essential for life - they are required for the biosynthesis of purine and pyrimidine bases and certain amino acids. Mammals obtain folate from their diets by an active transport system. In contrast, many microorganisms lack the active transport system and must synthesise folate de novo. Therefore, enzymes in the folate biosynthesis pathway, including HPPK, are target for developing antimicrobial agents.	Defined by 4 residues: ARG:A-82ARG:A-92ASP:A-95ASP:A-97 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.7.6.3 (PDB Primary Data) Search M-CSA Motif + EC 2.7.6.3

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.