6JWT

Crystal structure of Plasmodium falciparum HPPK-DHPS S436F/A437G/A613T triple mutant with Pteroate

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	HPPK	e6jwtB2	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)
B	Pterin_bind	e6jwtB1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Pterin_bind	ECOD (1.6)
A	HPPK	e6jwtA1	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)
A	Pterin_bind	e6jwtA2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Pterin_bind	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01288	7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK) (HPPK)	7,8-dihydro-6-hydroxymethylpterin-pyrophosphokinase (HPPK)	-	Domain
A, B	PF00809	Pterin binding enzyme (Pterin_bind)	Pterin binding enzyme	This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur p ...	This family includes a variety of pterin binding enzymes that all adopt a TIM barrel fold. The family includes dihydropteroate synthase EC:2.5.1.15 as well as a group methyltransferase enzymes including methyltetrahydrofolate, corrinoid iron-sulfur protein methyltransferase (MeTr) Swiss:Q46389 that catalyses a key step in the Wood-Ljungdahl pathway of carbon dioxide fixation. It transfers the N5-methyl group from methyltetrahydrofolate (CH3-H4folate) to a cob(I)amide centre in another protein, the corrinoid iron-sulfur protein. MeTr is a member of a family of proteins that includes methionine synthase and methanogenic enzymes that activate the methyl group of methyltetra-hydromethano(or -sarcino)pterin [2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase-dihydropteroate synthase	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding kinase activity transferase activity catalytic activity transferase activity, transferring phosphorus-containing groups 2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity diphosphotransferase activity dihydropteroate synthase activity transferase activity, transferring alkyl or aryl (other than methyl) groups cation binding metal ion binding	phosphorylation phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic 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 phosphorylation phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic 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 pteridine-containing compound metabolic process tetrahydrofolate biosynthetic process tetrahydrofolate metabolic process	membrane-bounded organelle intracellular organelle organelle envelope cellular anatomical structure intracellular anatomical structure mitochondrion mitochondrial envelope organelle cytoplasm intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR011005	Dihydropteroate synthase-like superfamily	Homologous Superfamily
A, B	IPR000550	7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase, HPPK	Domain
A, B	IPR006390	Dihydropteroate synthase domain	Domain
A, B	IPR000489	Pterin-binding domain	Domain
A, B	IPR035907	7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK superfamily	Homologous Superfamily
A, B	IPR045031	Dihydropteroate synthase-like	Family

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.