6B6U
Pyruvate Kinase M2 mutant - S437Y
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0003729 | molecular_function | mRNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004713 | molecular_function | protein tyrosine kinase activity |
| A | 0004743 | molecular_function | pyruvate kinase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005791 | cellular_component | rough endoplasmic reticulum |
| A | 0005829 | cellular_component | cytosol |
| A | 0005929 | cellular_component | cilium |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006417 | biological_process | regulation of translation |
| A | 0012501 | biological_process | programmed cell death |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0023026 | molecular_function | MHC class II protein complex binding |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0031982 | cellular_component | vesicle |
| A | 0032869 | biological_process | cellular response to insulin stimulus |
| A | 0034774 | cellular_component | secretory granule lumen |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061621 | biological_process | canonical glycolysis |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 1903561 | cellular_component | extracellular vesicle |
| A | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| A | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0003729 | molecular_function | mRNA binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004713 | molecular_function | protein tyrosine kinase activity |
| B | 0004743 | molecular_function | pyruvate kinase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005791 | cellular_component | rough endoplasmic reticulum |
| B | 0005829 | cellular_component | cytosol |
| B | 0005929 | cellular_component | cilium |
| B | 0006096 | biological_process | glycolytic process |
| B | 0006417 | biological_process | regulation of translation |
| B | 0012501 | biological_process | programmed cell death |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0023026 | molecular_function | MHC class II protein complex binding |
| B | 0030955 | molecular_function | potassium ion binding |
| B | 0031982 | cellular_component | vesicle |
| B | 0032869 | biological_process | cellular response to insulin stimulus |
| B | 0034774 | cellular_component | secretory granule lumen |
| B | 0045296 | molecular_function | cadherin binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0061621 | biological_process | canonical glycolysis |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 1903561 | cellular_component | extracellular vesicle |
| B | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
| B | 2000767 | biological_process | positive regulation of cytoplasmic translation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 601 |
| Chain | Residue |
| A | GLU272 |
| A | ASP296 |
| A | OXL602 |
| A | HOH785 |
| A | HOH926 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue OXL A 602 |
| Chain | Residue |
| A | GLY295 |
| A | ASP296 |
| A | THR328 |
| A | MG601 |
| A | HOH766 |
| A | HOH785 |
| A | HOH926 |
| A | HOH1057 |
| A | LYS270 |
| A | GLU272 |
| A | ALA293 |
| A | ARG294 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue K A 603 |
| Chain | Residue |
| A | ASN75 |
| A | SER77 |
| A | ASP113 |
| A | THR114 |
| A | SER243 |
| A | HOH878 |
| A | HOH1057 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CL A 604 |
| Chain | Residue |
| A | ASN44 |
| A | HIS464 |
| A | TYR466 |
| A | ILE469 |
| A | HOH795 |
| A | HOH923 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue SCN A 605 |
| Chain | Residue |
| A | HIS274 |
| A | PRO302 |
| A | LYS305 |
| A | HOH784 |
| A | HOH1041 |
| B | ILE35 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue SCN A 606 |
| Chain | Residue |
| A | LYS322 |
| A | HOH713 |
| A | HOH1032 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue SCN A 607 |
| Chain | Residue |
| A | LYS266 |
| A | LEU465 |
| A | TYR466 |
| A | HOH770 |
| A | HOH839 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | binding site for residue PEG A 608 |
| Chain | Residue |
| A | HIS252 |
| A | ALA286 |
| A | LYS505 |
| A | GLY506 |
| A | VAL530 |
| A | PRO531 |
| A | HOH702 |
| A | HOH764 |
| A | HOH894 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | binding site for residue B3P A 609 |
| Chain | Residue |
| A | ASP177 |
| A | ASP178 |
| A | LEU180 |
| A | LYS207 |
| A | GLN329 |
| A | GLU332 |
| A | GLY363 |
| A | HOH812 |
| A | HOH875 |
| A | HOH960 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 601 |
| Chain | Residue |
| B | GLU272 |
| B | ASP296 |
| B | OXL602 |
| B | HOH805 |
| B | HOH907 |
| site_id | AD2 |
| Number of Residues | 11 |
| Details | binding site for residue OXL B 602 |
| Chain | Residue |
| B | LYS270 |
| B | GLU272 |
| B | ALA293 |
| B | ARG294 |
| B | GLY295 |
| B | ASP296 |
| B | THR328 |
| B | MG601 |
| B | HOH756 |
| B | HOH805 |
| B | HOH907 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue K B 603 |
| Chain | Residue |
| B | ASN75 |
| B | SER77 |
| B | ASP113 |
| B | THR114 |
| B | HOH902 |
| B | HOH1098 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue CL B 604 |
| Chain | Residue |
| B | ASN44 |
| B | HIS464 |
| B | TYR466 |
| B | ILE469 |
| B | HOH816 |
| B | HOH861 |
| B | HOH1012 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue SCN B 605 |
| Chain | Residue |
| B | LYS266 |
| B | PRO323 |
| B | HIS439 |
| B | LEU465 |
| B | TYR466 |
| B | HOH845 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue SCN B 606 |
| Chain | Residue |
| B | HIS274 |
| B | PRO302 |
| B | LYS305 |
| B | HOH724 |
| A | ILE35 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue SCN B 607 |
| Chain | Residue |
| A | GLU82 |
| B | HIS252 |
| B | ARG255 |
| B | ALA286 |
| site_id | AD8 |
| Number of Residues | 12 |
| Details | binding site for residue PG4 B 608 |
| Chain | Residue |
| A | PHE26 |
| A | HOH966 |
| B | PHE26 |
| B | LEU353 |
| B | EDO609 |
| B | HOH705 |
| B | HOH733 |
| B | HOH945 |
| B | HOH976 |
| B | HOH980 |
| B | HOH1027 |
| B | HOH1029 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 609 |
| Chain | Residue |
| B | PHE26 |
| B | HIS29 |
| B | ALA388 |
| B | PG4608 |
| B | HOH884 |
| B | HOH980 |
| site_id | AE1 |
| Number of Residues | 14 |
| Details | binding site for residue B3P B 610 |
| Chain | Residue |
| A | LYS337 |
| B | ASP177 |
| B | ASP178 |
| B | LEU180 |
| B | LYS207 |
| B | GLN329 |
| B | GLU332 |
| B | GLY363 |
| B | HOH742 |
| B | HOH801 |
| B | HOH890 |
| B | HOH893 |
| B | HOH929 |
| B | HOH1031 |
Functional Information from PROSITE/UniProt
| site_id | PS00110 |
| Number of Residues | 13 |
| Details | PYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV |
| Chain | Residue | Details |
| A | ILE265-VAL277 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 88 |
| Details | Region: {"description":"Intersubunit contact"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23064226","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P30613","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23530218","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4FXF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 19 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15996096","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23530218","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1T5A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4FXF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Site: {"description":"Crucial for phosphotyrosine binding","evidences":[{"source":"PubMed","id":"27199445","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16964243","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17081983","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18088087","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18691976","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11980","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"21700219","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI22 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"4-hydroxyproline","evidences":[{"source":"PubMed","id":"21620138","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI23 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"30487609","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI24 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"24120661","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26787900","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI25 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI26 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI27 |
| Number of Residues | 6 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI28 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI29 |
| Number of Residues | 224 |
| Details | Region: {"description":"Interaction with POU5F1","evidences":[{"source":"PubMed","id":"18191611","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
