Protein family
Protein sequence
Protein function
Catalytic activity
EC number
EC number description
2.7.1.40
Transferases;
Transferring phosphorus-containing groups;
Phosphotransferases with an alcohol group as acceptor;
pyruvate kinase
2.7.10.2
Transferases;
Transferring phosphorus-containing groups;
Protein-tyrosine kinases;
non-specific protein-tyrosine kinase
2.7.11.1
Transferases;
Transferring phosphorus-containing groups;
Protein-serine/threonine kinases;
non-specific serine/threonine protein kinase
PDB | Resolution (Å) | PDB name |
---|---|---|
1T5A | 2.8 | Human Pyruvate Kinase M2 |
1ZJH | 2.2 | Structure of human muscle pyruvate kinase (PKM2) |
3BJF | 2.03 | Pyruvate kinase M2 is a phosphotyrosine binding protein |
3BJT | 2.5 | Pyruvate kinase M2 is a phosphotyrosine binding protein |
3G2G | 2.0 | S437Y Mutant of human muscle pyruvate kinase, isoform M2 |
3GQY | 1.85 | Activator-Bound Structure of Human Pyruvate Kinase M2 |
3GR4 | 1.6 | Activator-Bound Structure of Human Pyruvate Kinase M2 |
3H6O | 2.0 | Activator-Bound Structure of Human Pyruvate Kinase M2 |
3ME3 | 1.95 | Activator-Bound Structure of Human Pyruvate Kinase M2 |
3SRD | 2.902 | Human M2 pyruvate kinase in complex with fructose 1-6 bisphosphate and Oxalate. |
3SRF | 2.845 | Human M1 pyruvate kinase |
3SRH | 2.6 | Human M2 pyruvate kinase |
3U2Z | 2.1 | Activator-Bound Structure of Human Pyruvate Kinase M2 |
4B2D | 2.3 | human PKM2 with L-serine and FBP bound. |
4FXF | 2.55 | Structure of M2 pyruvate kinase in complex with phenylalanine |
4FXJ | 2.9 | Structure of M2 pyruvate kinase in complex with phenylalanine |
4G1N | 2.3 | PKM2 in complex with an activator |
4JPG | 2.33 | 2-((1H-benzo[d]imidazol-1-yl)methyl)-4H-pyrido[1,2-a]pyrimidin-4-ones as Novel PKM2 Activators |
4QG6 | 3.207 | crystal structure of PKM2-Y105E mutant |
4QG8 | 2.3 | crystal structure of PKM2-K305Q mutant |
4QG9 | 2.381 | crystal structure of PKM2-R399E mutant |
4QGC | 2.296 | crystal structure of PKM2-K422R mutant |
4RPP | 2.585 | crystal structure of PKM2-K422R mutant bound with FBP |
4WJ8 | 2.87 | Human Pyruvate Kinase M2 Mutant C424A |
4YJ5 | 2.41 | Crystal structure of PKM2 mutant |
5X0I | 2.64 | Crystal structure of PKM2 R399E mutant complexed with FBP and serine |
5X1V | 2.1 | PKM2 in complex with compound 2 |
5X1W | 3.0 | PKM2 in complex with compound 5 |
6B6U | 1.35 | Pyruvate Kinase M2 mutant - S437Y |
6GG3 | 3.72 | Crystal structure of M2 PYK in complex with Alanine. |
6GG4 | 2.46 | Crystal structure of M2 PYK in complex with Phenyalanine. |
6GG5 | 3.2 | Crystal structure of M2 PYK in complex with Tryptophan. |
6GG6 | 2.96 | Crystal structure of M2 PYK in complex with Serine. |
6JFB | 2.12 | Crystal structure of human pyruvate kinase M2 isoform |
6NU1 | 2.25 | Crystal Structure of Human PKM2 in Complex with L-cysteine |
6NU5 | 1.6 | Pyruvate Kinase M2 Mutant - S437Y in Complex with L-cysteine |
6NUB | 1.7 | Pyruvate Kinase M2 Mutant - S437Y in Complex with L-serine |
6TTF | 3.2 | PKM2 in complex with Compound 5 |
6TTH | 2.6 | PKM2 in complex with L-threonine |
6TTI | 2.5 | PKM2 in complex with Compound 6 |
6TTQ | 2.7 | PKM2 in complex with Compound 10 |
6V74 | 2.32 | Crystal Structure of Human PKM2 in Complex with L-asparagine |
6V75 | 2.85 | Crystal Structure of Human PKM2 in Complex with L-aspartate |
6V76 | 2.75 | Crystal Structure of Human PKM2 in Complex with L-valine |
6WP3 | 1.84 | Pyruvate Kinase M2 Mutant-K433Q |
6WP4 | 1.9 | Pyruvate Kinase M2 mutant-S37E |
6WP5 | 2.17 | Pyruvate Kinase M2 mutant-S37D |
6WP6 | 2.45 | Pyruvate Kinase M2 mutant-S37E K433E |
7L21 | 2.29 | Pyruvate Kinase M2 mutant-N70D |
8HMQ | 2.5 | Crystal Structure of PKM2 mutant P403A |
8HMR | 2.6 | Crystal Structure of PKM2 mutant L144P |
8HMS | 2.1 | Crystal Structure of PKM2 mutant C474S |
8HMU | 2.5 | Crystal Structure of PKM2 mutant R516C |
GO ontology | GO term | GO description |
---|---|---|
Biological Process | GO:0061621 | canonical glycolysis |
Biological Process | GO:0032869 | cellular response to insulin stimulus |
Biological Process | GO:0006096 | glycolytic process |
Biological Process | GO:0016310 | phosphorylation |
Biological Process | GO:2000767 | positive regulation of cytoplasmic translation |
Biological Process | GO:1903672 | positive regulation of sprouting angiogenesis |
Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
Biological Process | GO:0012501 | programmed cell death |
Molecular Function | GO:0005524 | ATP binding |
Molecular Function | GO:0023026 | MHC class II protein complex binding |
Molecular Function | GO:0003723 | RNA binding |
Molecular Function | GO:0045296 | cadherin binding |
Molecular Function | GO:0035402 | histone H3T11 kinase activity |
Molecular Function | GO:0003729 | mRNA binding |
Molecular Function | GO:0000287 | magnesium ion binding |
Molecular Function | GO:0030955 | potassium ion binding |
Molecular Function | GO:0042803 | protein homodimerization activity |
Molecular Function | GO:0004713 | protein tyrosine kinase activity |
Molecular Function | GO:0004743 | pyruvate kinase activity |
Molecular Function | GO:0003713 | transcription coactivator activity |
Cellular Component | GO:0005929 | cilium |
Cellular Component | GO:0062023 | collagen-containing extracellular matrix |
Cellular Component | GO:0005737 | cytoplasm |
Cellular Component | GO:0005829 | cytosol |
Cellular Component | GO:0070062 | extracellular exosome |
Cellular Component | GO:0005576 | extracellular region |
Cellular Component | GO:1903561 | extracellular vesicle |
Cellular Component | GO:1904813 | ficolin-1-rich granule lumen |
Cellular Component | GO:0005739 | mitochondrion |
Cellular Component | GO:0005634 | nucleus |
Cellular Component | GO:0005791 | rough endoplasmic reticulum |
Cellular Component | GO:0034774 | secretory granule lumen |
Cellular Component | GO:0031982 | vesicle |
InterPro | InterPro name |
---|---|
IPR001697 | Pyruvate kinase |
IPR011037 | Pyruvate kinase-like, insert domain superfamily |
IPR015793 | Pyruvate kinase, barrel |
IPR015795 | Pyruvate kinase, C-terminal |
IPR015806 | Pyruvate kinase, insert domain superfamily |
IPR015813 | Pyruvate/Phosphoenolpyruvate kinase-like domain superfamily |
IPR018209 | Pyruvate kinase, active site |
IPR036918 | Pyruvate kinase, C-terminal domain superfamily |
IPR040442 | Pyruvate kinase-like domain superfamily |
Pfam | Pfam name |
---|---|
PF00224 | Pyruvate kinase, barrel domain |
PF02887 | Pyruvate kinase, alpha/beta domain |
Reactome | Reactome Name | Node type | Reactome Root | Reactome Root Name |
---|---|---|---|---|
R-HSA-6798695 | Neutrophil degranulation | Leaf | R-HSA-168256 | Immune System |
R-HSA-70171 | Glycolysis | Internal node | R-HSA-1430728 | Metabolism |
Location | ECO term | Pubmed |
---|---|---|
Cytoplasm | ECO:0000269 | PubMed:25263439 |
Cytoplasm | ECO:0000269 | PubMed:26787900 |
Cytoplasm | ECO:0000269 | PubMed:32268273 |
Cytoplasm | ECO:0000305 | |
Nucleus | ECO:0000269 | PubMed:17308100 |
Nucleus | ECO:0000269 | PubMed:18191611 |
Nucleus | ECO:0000269 | PubMed:22056988 |
Nucleus | ECO:0000269 | PubMed:22901803 |
Nucleus | ECO:0000269 | PubMed:24120661 |
Nucleus | ECO:0000269 | PubMed:26787900 |
Nucleus | ECO:0000269 | PubMed:32268273 |