2VGB

HUMAN ERYTHROCYTE PYRUVATE KINASE

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
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
C	d2vgbc1	All beta proteins	PK beta-barrel domain-like	PK beta-barrel domain-like	Pyruvate kinase beta-barrel domain	Pyruvate kinase (PK)	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d2vgbc2	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Phosphoenolpyruvate/pyruvate domain	Pyruvate kinase	Pyruvate kinase, N-terminal domain	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d2vgbc3	Alpha and beta proteins (a/b)	Pyruvate kinase C-terminal domain-like	PK C-terminal domain-like	Pyruvate kinase, C-terminal domain	Pyruvate kinase, C-terminal domain	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d2vgbd1	All beta proteins	PK beta-barrel domain-like	PK beta-barrel domain-like	Pyruvate kinase beta-barrel domain	Pyruvate kinase (PK)	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d2vgbd2	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Phosphoenolpyruvate/pyruvate domain	Pyruvate kinase	Pyruvate kinase, N-terminal domain	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d2vgbd3	Alpha and beta proteins (a/b)	Pyruvate kinase C-terminal domain-like	PK C-terminal domain-like	Pyruvate kinase, C-terminal domain	Pyruvate kinase, C-terminal domain	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d2vgba1	All beta proteins	PK beta-barrel domain-like	PK beta-barrel domain-like	Pyruvate kinase beta-barrel domain	Pyruvate kinase (PK)	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d2vgba2	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Phosphoenolpyruvate/pyruvate domain	Pyruvate kinase	Pyruvate kinase, N-terminal domain	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d2vgba3	Alpha and beta proteins (a/b)	Pyruvate kinase C-terminal domain-like	PK C-terminal domain-like	Pyruvate kinase, C-terminal domain	Pyruvate kinase, C-terminal domain	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d2vgbb1	All beta proteins	PK beta-barrel domain-like	PK beta-barrel domain-like	Pyruvate kinase beta-barrel domain	Pyruvate kinase (PK)	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d2vgbb2	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Phosphoenolpyruvate/pyruvate domain	Pyruvate kinase	Pyruvate kinase, N-terminal domain	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d2vgbb3	Alpha and beta proteins (a/b)	Pyruvate kinase C-terminal domain-like	PK C-terminal domain-like	Pyruvate kinase, C-terminal domain	Pyruvate kinase, C-terminal domain	HUMAN (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	PK beta-barrel domain-like	8043047	3001296	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Phosphoenolpyruvate/pyruvate domain	8043048	3000510	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	PK C-terminal domain-like	8043050	3000442	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Phosphoenolpyruvate/pyruvate domain	8043048	3000510	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Phosphoenolpyruvate/pyruvate domain	8043048	3000510	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Phosphoenolpyruvate/pyruvate domain	8043048	3000510	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	PK C-terminal domain-like	8043050	3000442	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	PK beta-barrel domain-like	8043047	3001296	SCOP2B (2022-06-29)
A	SCOP2 Family	Pyruvate kinase beta-barrel domain	8030668	4002474	SCOP2 (2022-06-29)
A	SCOP2 Family	Pyruvate kinase	8030669	4003255	SCOP2 (2022-06-29)
A	SCOP2 Family	PK C-terminal domain-like	8030671	4000500	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PK beta-barrel domain-like	8043047	3001296	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Phosphoenolpyruvate/pyruvate domain	8043048	3000510	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PK C-terminal domain-like	8043050	3000442	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Phosphoenolpyruvate/pyruvate domain	8043048	3000510	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Phosphoenolpyruvate/pyruvate domain	8043048	3000510	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	PK C-terminal domain-like	8043050	3000442	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)
C	PK_2nd	e2vgbC1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: PK beta-barrel domain-like	F: PK_2nd	ECOD (1.6)
C	PK_1st	e2vgbC2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PK_1st	ECOD (1.6)
C	PK_C	e2vgbC3	A: a/b three-layered sandwiches	X: PK C-terminal domain-like (From Topology)	H: PK C-terminal domain-like (From Topology)	T: PK C-terminal domain-like	F: PK_C	ECOD (1.6)
D	PK_2nd	e2vgbD4	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: PK beta-barrel domain-like	F: PK_2nd	ECOD (1.6)
D	PK_1st	e2vgbD3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PK_1st	ECOD (1.6)
D	PK_C	e2vgbD1	A: a/b three-layered sandwiches	X: PK C-terminal domain-like (From Topology)	H: PK C-terminal domain-like (From Topology)	T: PK C-terminal domain-like	F: PK_C	ECOD (1.6)
A	PK_2nd	e2vgbA3	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: PK beta-barrel domain-like	F: PK_2nd	ECOD (1.6)
A	PK_1st	e2vgbA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PK_1st	ECOD (1.6)
A	PK_C	e2vgbA4	A: a/b three-layered sandwiches	X: PK C-terminal domain-like (From Topology)	H: PK C-terminal domain-like (From Topology)	T: PK C-terminal domain-like	F: PK_C	ECOD (1.6)
B	PK_2nd	e2vgbB3	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: PK beta-barrel domain-like	F: PK_2nd	ECOD (1.6)
B	PK_1st	e2vgbB2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PK_1st	ECOD (1.6)
B	PK_C	e2vgbB1	A: a/b three-layered sandwiches	X: PK C-terminal domain-like (From Topology)	H: PK C-terminal domain-like (From Topology)	T: PK C-terminal domain-like	F: PK_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	3.40.1380.20	Alpha Beta	3-Layer(aba) Sandwich	Pyruvate Kinase	Chain: A, domain 1	CATH (4.3.0)
C	3.20.20.60	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Phosphoenolpyruvate-binding domains	CATH (4.3.0)
C	2.40.33.10	Mainly Beta	Beta Barrel	M1 Pyruvate Kinase	Domain 3	CATH (4.3.0)
D	3.40.1380.20	Alpha Beta	3-Layer(aba) Sandwich	Pyruvate Kinase	Chain: A, domain 1	CATH (4.3.0)
D	3.20.20.60	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Phosphoenolpyruvate-binding domains	CATH (4.3.0)
D	2.40.33.10	Mainly Beta	Beta Barrel	M1 Pyruvate Kinase	Domain 3	CATH (4.3.0)
A	3.40.1380.20	Alpha Beta	3-Layer(aba) Sandwich	Pyruvate Kinase	Chain: A, domain 1	CATH (4.3.0)
A	3.20.20.60	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Phosphoenolpyruvate-binding domains	CATH (4.3.0)
A	2.40.33.10	Mainly Beta	Beta Barrel	M1 Pyruvate Kinase	Domain 3	CATH (4.3.0)
B	3.40.1380.20	Alpha Beta	3-Layer(aba) Sandwich	Pyruvate Kinase	Chain: A, domain 1	CATH (4.3.0)
B	3.20.20.60	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Phosphoenolpyruvate-binding domains	CATH (4.3.0)
B	2.40.33.10	Mainly Beta	Beta Barrel	M1 Pyruvate Kinase	Domain 3	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF02887	Pyruvate kinase, alpha/beta domain (PK_C)	Pyruvate kinase, alpha/beta domain	Pyruvate kinase catalyses the final step in glycolysis, the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP [1,2]. The structure of several pyruvate kinases from various organisms have been determined [2, ...	Pyruvate kinase catalyses the final step in glycolysis, the conversion of phosphoenolpyruvate to pyruvate with concomitant phosphorylation of ADP to ATP [1,2]. The structure of several pyruvate kinases from various organisms have been determined [2, 3,4]. The protein comprises three-four domains: a small N-terminal helical domain (absent in bacterial PK), a beta/alpha barrel domain, a beta-barrel domain (inserted within the beta/alpha-barrel domain), and a 3-layer alpha/beta/alpha sandwich domain (represented in this entry). This domain is at the C-terminal of pyruvate kinases and contains the FBP (fructose 1,6-bisphosphate) binding site [2,4,5].	Domain
A, B, C, D	PF00224	Pyruvate kinase, barrel domain (PK)	Pyruvate kinase, barrel domain	This is the barrel domain of pyruvate kinases. This domain represents the beta/alpha barrel and the small beta-barrel domain inserted within it. The active site is found in a cleft between the two domains [1,2,3,4].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	PYRUVATE KINASE ISOZYMES R/L	cation binding ion binding binding potassium ion binding alkali metal ion binding metal ion binding small molecule binding kinase activity transferase activity catalytic activity transferase activity, transferring phosphorus-containing groups monosaccharide binding carbohydrate binding magnesium ion binding cation binding ion binding binding potassium ion binding alkali metal ion binding metal ion binding small molecule binding kinase activity transferase activity catalytic activity transferase activity, transferring phosphorus-containing groups monosaccharide binding carbohydrate binding magnesium ion 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 pyruvate kinase activity phosphotransferase activity, alcohol group as acceptor	response to stimulus response to metal ion response to chemical response to hexose response to monosaccharide response to carbohydrate response to glucose response to oxygen-containing compound cellular response to stimulus cellular response to chemical stimulus response to epinephrine cellular response to epinephrine stimulus cellular process ribonucleotide catabolic process response to stimulus response to metal ion response to chemical response to hexose response to monosaccharide response to carbohydrate response to glucose response to oxygen-containing compound cellular response to stimulus cellular response to chemical stimulus response to epinephrine cellular response to epinephrine stimulus cellular process ribonucleotide catabolic process pyridine nucleotide catabolic process oxoacid metabolic process carbohydrate catabolic process carbohydrate derivative metabolic process organophosphate catabolic process nucleoside phosphate catabolic process organic acid metabolic process nucleobase-containing compound metabolic process glycolytic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process small molecule metabolic process purine ribonucleotide catabolic process phosphorus metabolic process pyridine nucleotide metabolic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process pyruvate metabolic process cellular metabolic process purine nucleoside diphosphate metabolic process primary metabolic process purine-containing compound catabolic process nucleotide metabolic process nucleobase-containing compound catabolic process nucleoside diphosphate metabolic process purine nucleoside diphosphate catabolic process nucleoside diphosphate catabolic process metabolic 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 ADP catabolic process carboxylic acid metabolic process generation of precursor metabolites and energy purine-containing compound metabolic process ADP metabolic process organophosphate metabolic process purine ribonucleoside diphosphate metabolic process purine ribonucleoside diphosphate catabolic process response to organophosphorus response to nitrogen compound response to ATP response to purine-containing compound response to organic cyclic compound response to decreased oxygen levels response to hypoxia response to stress response to oxygen levels response to abiotic stimulus response to cAMP cellular response to nitrogen compound response to endogenous stimulus response to peptide hormone cellular response to peptide hormone stimulus cellular response to oxygen-containing compound cellular response to endogenous stimulus response to hormone response to insulin cellular response to insulin stimulus cellular response to hormone stimulus response to nutrient levels response to nutrient monocarboxylic acid biosynthetic process small molecule biosynthetic process cellular biosynthetic process organic acid biosynthetic process carboxylic acid biosynthetic process biosynthetic process pyruvate biosynthetic process	extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol transferase complex, transferring phosphorus-containing groups extracellular exosome membrane-bounded organelle extracellular vesicle extracellular organelle extracellular region organelle extracellular space cellular anatomical entity vesicle extracellular membrane-bounded organelle intracellular anatomical structure cytoplasm cytosol transferase complex, transferring phosphorus-containing groups protein-containing complex pyruvate kinase complex catalytic complex transferase complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR011037	Pyruvate kinase-like, insert domain superfamily	Homologous Superfamily
A, B, C, D	IPR015806	Pyruvate kinase, insert domain superfamily	Homologous Superfamily
A, B, C, D	IPR036918	Pyruvate kinase, C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR040442	Pyruvate kinase-like domain superfamily	Homologous Superfamily
A, B, C, D	IPR015793	Pyruvate kinase, barrel	Domain
A, B, C, D	IPR015795	Pyruvate kinase, C-terminal	Domain
A, B, C, D	IPR015813	Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily	Homologous Superfamily
A, B, C, D	IPR001697	Pyruvate kinase	Family
A, B, C, D	IPR018209	Pyruvate kinase, active site	Active Site

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D	Pharos: P30613	pyruvate kinase deficiency of red cells pyruvate kinase hyperactivity Liver Cirrhosis, Experimental familial hemolytic anemia Crohn disease glioblastoma psoriasis brain aneurysm hemolytic anemia malignant mesothelioma congenital anemia gastric adenocarcinoma large cell medulloblastoma osteosarcoma

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.