8F5U
Rabbit muscle pyruvate kinase in complex with magnesium, potassium and pyruvate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion 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 | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005791 | cellular_component | rough endoplasmic reticulum |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006417 | biological_process | regulation of translation |
| A | 0016301 | molecular_function | kinase activity |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0032869 | biological_process | cellular response to insulin stimulus |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| A | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| B | 0000287 | molecular_function | magnesium ion 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 | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005791 | cellular_component | rough endoplasmic reticulum |
| B | 0006096 | biological_process | glycolytic process |
| B | 0006417 | biological_process | regulation of translation |
| B | 0016301 | molecular_function | kinase activity |
| B | 0030955 | molecular_function | potassium ion binding |
| B | 0032869 | biological_process | cellular response to insulin stimulus |
| B | 0046872 | molecular_function | metal ion binding |
| B | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| B | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003729 | molecular_function | mRNA binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004713 | molecular_function | protein tyrosine kinase activity |
| C | 0004743 | molecular_function | pyruvate kinase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005791 | cellular_component | rough endoplasmic reticulum |
| C | 0006096 | biological_process | glycolytic process |
| C | 0006417 | biological_process | regulation of translation |
| C | 0016301 | molecular_function | kinase activity |
| C | 0030955 | molecular_function | potassium ion binding |
| C | 0032869 | biological_process | cellular response to insulin stimulus |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| C | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003729 | molecular_function | mRNA binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004713 | molecular_function | protein tyrosine kinase activity |
| D | 0004743 | molecular_function | pyruvate kinase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005634 | cellular_component | nucleus |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005791 | cellular_component | rough endoplasmic reticulum |
| D | 0006096 | biological_process | glycolytic process |
| D | 0006417 | biological_process | regulation of translation |
| D | 0016301 | molecular_function | kinase activity |
| D | 0030955 | molecular_function | potassium ion binding |
| D | 0032869 | biological_process | cellular response to insulin stimulus |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| D | 2000767 | biological_process | positive regulation of cytoplasmic translation |
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 | ILE264-VAL276 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 56 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | ASN69 | |
| A | ASN74 | |
| A | SER76 | |
| A | ARG105 | |
| A | ASP112 | |
| A | THR113 | |
| A | ARG119 | |
| A | LYS206 | |
| A | GLU271 | |
| A | THR431 | |
| A | HIS463 | |
| A | TRP481 | |
| A | ARG488 | |
| A | ARG515 | |
| B | ASN69 | |
| B | ASN74 | |
| B | SER76 | |
| B | ARG105 | |
| B | ASP112 | |
| B | THR113 | |
| B | ARG119 | |
| B | LYS206 | |
| B | GLU271 | |
| B | THR431 | |
| B | HIS463 | |
| B | TRP481 | |
| B | ARG488 | |
| B | ARG515 | |
| C | ASN69 | |
| C | ASN74 | |
| C | SER76 | |
| C | ARG105 | |
| C | ASP112 | |
| C | THR113 | |
| C | ARG119 | |
| C | LYS206 | |
| C | GLU271 | |
| C | THR431 | |
| C | HIS463 | |
| C | TRP481 | |
| C | ARG488 | |
| C | ARG515 | |
| D | ASN69 | |
| D | ASN74 | |
| D | SER76 | |
| D | ARG105 | |
| D | ASP112 | |
| D | THR113 | |
| D | ARG119 | |
| D | LYS206 | |
| D | GLU271 | |
| D | THR431 | |
| D | HIS463 | |
| D | TRP481 | |
| D | ARG488 | |
| D | ARG515 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P30613 |
| Chain | Residue | Details |
| A | ARG72 | |
| A | LYS269 | |
| A | GLY294 | |
| A | ASP295 | |
| A | THR327 | |
| B | ARG72 | |
| B | LYS269 | |
| B | GLY294 | |
| B | ASP295 | |
| B | THR327 | |
| C | ARG72 | |
| C | LYS269 | |
| C | GLY294 | |
| C | ASP295 | |
| C | THR327 | |
| D | ARG72 | |
| D | LYS269 | |
| D | GLY294 | |
| D | ASP295 | |
| D | THR327 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Transition state stabilizer => ECO:0000250|UniProtKB:P00549 |
| Chain | Residue | Details |
| A | LYS269 | |
| B | LYS269 | |
| C | LYS269 | |
| D | LYS269 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P11979 |
| Chain | Residue | Details |
| A | SER1 | |
| B | SER1 | |
| C | SER1 | |
| D | SER1 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | LYS2 | |
| B | LYS2 | |
| C | LYS2 | |
| D | LYS2 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | SER36 | |
| A | SER126 | |
| B | SER36 | |
| B | SER126 | |
| C | SER36 | |
| C | SER126 | |
| D | SER36 | |
| D | SER126 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | THR40 | |
| A | THR194 | |
| B | THR40 | |
| B | THR194 | |
| C | THR40 | |
| C | THR194 | |
| D | THR40 | |
| D | THR194 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | LYS61 | |
| A | LYS88 | |
| A | LYS304 | |
| B | LYS61 | |
| B | LYS88 | |
| B | LYS304 | |
| C | LYS61 | |
| C | LYS88 | |
| C | LYS304 | |
| D | LYS61 | |
| D | LYS88 | |
| D | LYS304 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | LYS65 | |
| A | LYS497 | |
| B | LYS65 | |
| B | LYS497 | |
| C | LYS65 | |
| C | LYS497 | |
| D | LYS65 | |
| D | LYS497 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P11980 |
| Chain | Residue | Details |
| A | SER96 | |
| A | SER99 | |
| B | SER96 | |
| B | SER99 | |
| C | SER96 | |
| C | SER99 | |
| D | SER96 | |
| D | SER99 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | TYR104 | |
| A | TYR174 | |
| B | TYR104 | |
| B | TYR174 | |
| C | TYR104 | |
| C | TYR174 | |
| D | TYR104 | |
| D | TYR174 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | TYR147 | |
| B | TYR147 | |
| C | TYR147 | |
| D | TYR147 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | LYS165 | |
| A | LYS321 | |
| B | LYS165 | |
| B | LYS321 | |
| C | LYS165 | |
| C | LYS321 | |
| D | LYS165 | |
| D | LYS321 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | LYS265 | |
| B | LYS265 | |
| C | LYS265 | |
| D | LYS265 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | LYS269 | |
| B | LYS269 | |
| C | LYS269 | |
| D | LYS269 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P52480 |
| Chain | Residue | Details |
| A | LYS474 | |
| B | LYS474 | |
| C | LYS474 | |
| D | LYS474 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | LYS114 | |
| B | LYS114 | |
| C | LYS114 | |
| D | LYS114 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 12 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | LYS265 | |
| A | LYS269 | |
| B | LYS265 | |
| B | LYS269 | |
| C | LYS265 | |
| C | LYS269 | |
| D | LYS265 | |
| D | LYS269 |
| site_id | SWS_FT_FI19 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0000250|UniProtKB:P14618 |
| Chain | Residue | Details |
| A | LYS165 | |
| B | LYS165 | |
| C | LYS165 | |
| D | LYS165 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| A | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| A | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| A | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| A | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| B | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| B | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| B | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| B | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| C | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| C | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| C | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| C | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| D | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| D | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| D | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| D | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
