1PFK

CRYSTAL STRUCTURE OF THE COMPLEX OF PHOSPHOFRUCTOKINASE FROM ESCHERICHIA COLI WITH ITS REACTION PRODUCTS

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	d1pfka_	Alpha and beta proteins (a/b)	Phosphofructokinase	Phosphofructokinase	Phosphofructokinase	ATP-dependent phosphofructokinase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1pfkb_	Alpha and beta proteins (a/b)	Phosphofructokinase	Phosphofructokinase	Phosphofructokinase	ATP-dependent phosphofructokinase	(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	Phosphofructokinase	8020844	4000837	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Phosphofructokinase	8033224	3001648	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Phosphofructokinase	8033224	3001648	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	PFK_N	e1pfkA2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Phosphofructokinase N-terminal domain	F: PFK_N	ECOD (1.6)
A	PFK_C	e1pfkA3	A: a/b three-layered sandwiches	X: Phosphofructokinase C-terminal domain (From Topology)	H: Phosphofructokinase C-terminal domain (From Topology)	T: Phosphofructokinase C-terminal domain	F: PFK_C	ECOD (1.6)
B	PFK_N	e1pfkB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Phosphofructokinase N-terminal domain	F: PFK_N	ECOD (1.6)
B	PFK_C	e1pfkB2	A: a/b three-layered sandwiches	X: Phosphofructokinase C-terminal domain (From Topology)	H: Phosphofructokinase C-terminal domain (From Topology)	T: Phosphofructokinase C-terminal domain	F: PFK_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.450	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
A	3.40.50.460	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Phosphofructokinase domain	CATH (4.3.0)
B	3.40.50.450	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	3.40.50.460	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Phosphofructokinase domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00365	Phosphofructokinase (PFK)	Phosphofructokinase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PHOSPHOFRUCTOKINASE	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 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 guanyl nucleotide binding GDP binding guanyl ribonucleotide binding fructose-6-phosphate binding carbohydrate kinase activity kinase activity phosphofructokinase activity 6-phosphofructokinase activity transferase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups AMP binding monosaccharide binding carbohydrate binding identical protein binding protein binding	organic substance metabolic process organophosphate metabolic process cellular metabolic process phosphate-containing compound metabolic process fructose 6-phosphate metabolic process carbohydrate derivative metabolic process metabolic process cellular process phosphorus metabolic process ribonucleotide catabolic process pyridine nucleotide catabolic process oxoacid metabolic process carbohydrate catabolic process organophosphate catabolic process organic substance metabolic process organophosphate metabolic process cellular metabolic process phosphate-containing compound metabolic process fructose 6-phosphate metabolic process carbohydrate derivative metabolic process metabolic process cellular process phosphorus metabolic process ribonucleotide catabolic process pyridine nucleotide catabolic process oxoacid metabolic process carbohydrate catabolic process organophosphate catabolic process nucleoside phosphate catabolic process organic acid metabolic process nucleobase-containing compound metabolic process glycolytic process pyridine-containing compound metabolic process small molecule metabolic process purine ribonucleotide catabolic process pyridine nucleotide metabolic process nucleoside phosphate metabolic process organonitrogen compound catabolic process nicotinamide nucleotide metabolic process pyruvate metabolic process purine nucleoside diphosphate metabolic process primary metabolic process purine-containing compound catabolic process nucleotide metabolic process nucleobase-containing compound catabolic process organic cyclic compound metabolic process nucleoside diphosphate metabolic process purine nucleoside diphosphate catabolic process nucleoside diphosphate catabolic process nucleoside triphosphate metabolic process monocarboxylic acid metabolic process purine ribonucleotide metabolic process pyridine-containing compound catabolic process ribose phosphate metabolic process catabolic process ATP metabolic process purine nucleotide metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process purine ribonucleoside triphosphate metabolic process ribonucleoside diphosphate metabolic process ribonucleoside diphosphate catabolic process nucleotide catabolic process ribonucleoside triphosphate metabolic process purine nucleoside triphosphate metabolic process purine nucleotide catabolic process carbohydrate metabolic process carbohydrate derivative catabolic process organonitrogen compound metabolic process ADP catabolic process carboxylic acid metabolic process generation of precursor metabolites and energy organic cyclic compound catabolic process purine-containing compound metabolic process ADP metabolic process purine ribonucleoside diphosphate metabolic process organic substance catabolic process purine ribonucleoside diphosphate catabolic process monosaccharide metabolic process hexose catabolic process hexose metabolic process glucose catabolic process monosaccharide catabolic process small molecule catabolic process glucose metabolic process fructose 1,6-bisphosphate metabolic process protein-containing complex organization protein homotetramerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein tetramerization protein-containing complex assembly protein homooligomerization cellular component organization or biogenesis NADH regeneration glucose catabolic process to pyruvate NADH metabolic process canonical glycolysis NAD metabolic process glycolytic process through glucose-6-phosphate NAD catabolic process glycolytic process through fructose-6-phosphate	transferase complex, transferring phosphorus-containing groups protein-containing complex intracellular anatomical structure catalytic complex transferase complex cytoplasm cellular anatomical entity cytosol 6-phosphofructokinase complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR012828	ATP-dependent 6-phosphofructokinase, prokaryotic	Family
A, B	IPR035966	Phosphofructokinase superfamily	Homologous Superfamily
A, B	IPR000023	Phosphofructokinase domain	Domain
A, B	IPR012003	ATP-dependent 6-phosphofructokinase, prokaryotic-type	Family
A, B	IPR022953	ATP-dependent 6-phosphofructokinase	Family
A, B	IPR015912	Phosphofructokinase, conserved site	Conserved Site

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

Chains	Enzyme Name	Description	Catalytic Residues
A	Phosphofructokinase I M-CSA #365	Phosphofructokinase (PFK) is a key enzyme in glycolysis. It transfers a phosphate group to fructose and in doing so controls entry into the pathway. PFK is highly regulated and is cooperative for fructose and shows allosteric inhibition by phosphoenolpyruvate and activation by ADP. The enzyme changes from the R state to the T state by a rotation around the 'p' axis of the molecule, resulting in a change in the subunit-subunit interactions that are communicated to the active site. The ATP binding site remains fixed during the transition from R to T state except for the residue arg 72 that is important for bridging the substrate phosphates during catalysis. In the T state this Arg residue forms a salt bridge with glu241. The T state is also characterised by a large change in the substrate binding site, the movement of the '6-F' loop leads to the collapse of this binding site.	Defined by 7 residues: GLY:A-12 [auth A-11]ARG:A-73 [auth A-72]ASP:A-104 [auth A-103]THR:A-126 [auth A-125]ASP:A-128 [auth A-127]ASP:A-130 [auth A-129]ARG:A-172 [auth A-171] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.7.1.11 (PDB Primary Data) Search M-CSA Motif + EC 2.7.1.11

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.