5ETL

E. coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase complexed with AMPCPP and inhibitor at 1.82 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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d5etlb1	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)
B	d5etlb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
D	d5etld1	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)
D	d5etld2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
A	d5etla1	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)
A	d5etla2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d5etlc1	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)
C	d5etlc2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(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)
B	SCOP2B Superfamily	6-hydroxymethyl-7 8-dihydropterin pyrophosphokinase HPPK	8044430	3001294	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	6-hydroxymethyl-7 8-dihydropterin pyrophosphokinase HPPK	8044430	3001294	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	6-hydroxymethyl-7 8-dihydropterin pyrophosphokinase HPPK	8044430	3001294	SCOP2B (2022-06-29)
C	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)
B	PF01288	e5etlB1	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: PF01288	ECOD (1.6)
D	PF01288	e5etlD1	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: PF01288	ECOD (1.6)
A	PF01288	e5etlA1	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: PF01288	ECOD (1.6)
C	PF01288	e5etlC1	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: PF01288	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.30.70.560	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK	CATH (4.3.0)
D	3.30.70.560	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK	CATH (4.3.0)
A	3.30.70.560	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK	CATH (4.3.0)
C	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, B, C, D	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, B, C, D	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	phosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic 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 organic substance metabolic process phosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic 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 organic substance metabolic process organic substance 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 dicarboxylic acid metabolic process carboxylic acid metabolic process amide biosynthetic process cellular modified amino acid metabolic process vitamin metabolic process organic cyclic compound metabolic process biosynthetic process cellular modified amino acid biosynthetic process organic cyclic compound biosynthetic process folic acid-containing compound metabolic process pteridine-containing compound biosynthetic process pteridine-containing compound metabolic process tetrahydrofolate biosynthetic process tetrahydrofolate metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

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

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.