3N25
The structure of muscle pyruvate kinase in complex with proline, pyruvate, and Mn2+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003729 | molecular_function | mRNA binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0004713 | molecular_function | protein tyrosine kinase activity |
| A | 0004715 | molecular_function | non-membrane spanning 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 | 0016740 | molecular_function | transferase activity |
| A | 0030955 | molecular_function | potassium ion binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003729 | molecular_function | mRNA binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0004713 | molecular_function | protein tyrosine kinase activity |
| B | 0004715 | molecular_function | non-membrane spanning 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 | 0016740 | molecular_function | transferase activity |
| B | 0030955 | molecular_function | potassium ion binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003729 | molecular_function | mRNA binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0004713 | molecular_function | protein tyrosine kinase activity |
| C | 0004715 | molecular_function | non-membrane spanning 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 | 0016740 | molecular_function | transferase activity |
| C | 0030955 | molecular_function | potassium ion binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003729 | molecular_function | mRNA binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004674 | molecular_function | protein serine/threonine kinase activity |
| D | 0004713 | molecular_function | protein tyrosine kinase activity |
| D | 0004715 | molecular_function | non-membrane spanning 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 | 0016740 | molecular_function | transferase activity |
| D | 0030955 | molecular_function | potassium ion binding |
| 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 |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0003729 | molecular_function | mRNA binding |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004674 | molecular_function | protein serine/threonine kinase activity |
| E | 0004713 | molecular_function | protein tyrosine kinase activity |
| E | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| E | 0004743 | molecular_function | pyruvate kinase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005524 | molecular_function | ATP binding |
| E | 0005634 | cellular_component | nucleus |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005791 | cellular_component | rough endoplasmic reticulum |
| E | 0006096 | biological_process | glycolytic process |
| E | 0006417 | biological_process | regulation of translation |
| E | 0016301 | molecular_function | kinase activity |
| E | 0016740 | molecular_function | transferase activity |
| E | 0030955 | molecular_function | potassium ion binding |
| E | 0046872 | molecular_function | metal ion binding |
| E | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| E | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| F | 0000166 | molecular_function | nucleotide binding |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0003729 | molecular_function | mRNA binding |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004674 | molecular_function | protein serine/threonine kinase activity |
| F | 0004713 | molecular_function | protein tyrosine kinase activity |
| F | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| F | 0004743 | molecular_function | pyruvate kinase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005524 | molecular_function | ATP binding |
| F | 0005634 | cellular_component | nucleus |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005791 | cellular_component | rough endoplasmic reticulum |
| F | 0006096 | biological_process | glycolytic process |
| F | 0006417 | biological_process | regulation of translation |
| F | 0016301 | molecular_function | kinase activity |
| F | 0016740 | molecular_function | transferase activity |
| F | 0030955 | molecular_function | potassium ion binding |
| F | 0046872 | molecular_function | metal ion binding |
| F | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| F | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0003729 | molecular_function | mRNA binding |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0004674 | molecular_function | protein serine/threonine kinase activity |
| G | 0004713 | molecular_function | protein tyrosine kinase activity |
| G | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| G | 0004743 | molecular_function | pyruvate kinase activity |
| G | 0005515 | molecular_function | protein binding |
| G | 0005524 | molecular_function | ATP binding |
| G | 0005634 | cellular_component | nucleus |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0005791 | cellular_component | rough endoplasmic reticulum |
| G | 0006096 | biological_process | glycolytic process |
| G | 0006417 | biological_process | regulation of translation |
| G | 0016301 | molecular_function | kinase activity |
| G | 0016740 | molecular_function | transferase activity |
| G | 0030955 | molecular_function | potassium ion binding |
| G | 0046872 | molecular_function | metal ion binding |
| G | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| G | 2000767 | biological_process | positive regulation of cytoplasmic translation |
| H | 0000166 | molecular_function | nucleotide binding |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0003729 | molecular_function | mRNA binding |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0004674 | molecular_function | protein serine/threonine kinase activity |
| H | 0004713 | molecular_function | protein tyrosine kinase activity |
| H | 0004715 | molecular_function | non-membrane spanning protein tyrosine kinase activity |
| H | 0004743 | molecular_function | pyruvate kinase activity |
| H | 0005515 | molecular_function | protein binding |
| H | 0005524 | molecular_function | ATP binding |
| H | 0005634 | cellular_component | nucleus |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0005791 | cellular_component | rough endoplasmic reticulum |
| H | 0006096 | biological_process | glycolytic process |
| H | 0006417 | biological_process | regulation of translation |
| H | 0016301 | molecular_function | kinase activity |
| H | 0016740 | molecular_function | transferase activity |
| H | 0030955 | molecular_function | potassium ion binding |
| H | 0046872 | molecular_function | metal ion binding |
| H | 1903672 | biological_process | positive regulation of sprouting angiogenesis |
| H | 2000767 | biological_process | positive regulation of cytoplasmic translation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PRO A 1200 |
| Chain | Residue |
| A | ARG42 |
| A | HOH1265 |
| A | ASN43 |
| A | ASN69 |
| A | ARG105 |
| A | HIS463 |
| A | TYR465 |
| A | ILE468 |
| A | PHE469 |
| A | PRO470 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PRO B 1600 |
| Chain | Residue |
| B | ARG42 |
| B | ASN43 |
| B | ASN69 |
| B | HIS463 |
| B | ILE468 |
| B | PHE469 |
| B | PRO470 |
| B | HOH769 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PRO C 1600 |
| Chain | Residue |
| C | ARG42 |
| C | ASN43 |
| C | GLY45 |
| C | ASN69 |
| C | ARG105 |
| C | HIS463 |
| C | ILE468 |
| C | PHE469 |
| C | PRO470 |
| C | HOH1638 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PRO D 1600 |
| Chain | Residue |
| D | ARG42 |
| D | ASN43 |
| D | ASN69 |
| D | ARG105 |
| D | HIS463 |
| D | ILE468 |
| D | PHE469 |
| D | PRO470 |
| D | HOH1419 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PRO E 1600 |
| Chain | Residue |
| E | ARG42 |
| E | ASN43 |
| E | ASN69 |
| E | ARG105 |
| E | HIS463 |
| E | ILE468 |
| E | PHE469 |
| E | PRO470 |
| E | HOH990 |
| E | HOH1421 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PRO F 1600 |
| Chain | Residue |
| F | ARG42 |
| F | ASN43 |
| F | ASN69 |
| F | ARG105 |
| F | HIS463 |
| F | TYR465 |
| F | ILE468 |
| F | PHE469 |
| F | PRO470 |
| F | HOH1422 |
| F | HOH1622 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PRO G 1600 |
| Chain | Residue |
| G | ARG42 |
| G | ASN43 |
| G | ASN69 |
| G | ARG105 |
| G | HIS463 |
| G | TYR465 |
| G | ILE468 |
| G | PHE469 |
| G | PRO470 |
| G | HOH922 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PRO H 1600 |
| Chain | Residue |
| H | ARG42 |
| H | ASN43 |
| H | ASN69 |
| H | ARG105 |
| H | HIS463 |
| H | TYR465 |
| H | ILE468 |
| H | PHE469 |
| H | PRO470 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 640 |
| Chain | Residue |
| A | GLU271 |
| A | ASP295 |
| A | PYR1000 |
| A | HOH1225 |
| A | HOH1275 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PYR A 1000 |
| Chain | Residue |
| A | ARG72 |
| A | LYS269 |
| A | GLU271 |
| A | ALA292 |
| A | ARG293 |
| A | GLY294 |
| A | ASP295 |
| A | THR327 |
| A | MN640 |
| A | HOH1214 |
| A | HOH1225 |
| A | HOH1275 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 1100 |
| Chain | Residue |
| A | HOH1069 |
| A | ASN74 |
| A | SER76 |
| A | ASP112 |
| A | THR113 |
| A | HOH765 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 1300 |
| Chain | Residue |
| A | LYS124 |
| A | GLY125 |
| A | SER126 |
| A | GLY127 |
| A | THR128 |
| A | HOH1392 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE NA A 2100 |
| Chain | Residue |
| A | THR431 |
| A | SER433 |
| A | SER436 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 6002 |
| Chain | Residue |
| A | ARG42 |
| A | LYS65 |
| A | SER66 |
| A | GLY67 |
| A | HIS378 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 6043 |
| Chain | Residue |
| A | GLU95 |
| A | TYR104 |
| A | HIS456 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 6050 |
| Chain | Residue |
| A | GLU284 |
| A | ALA285 |
| A | SER286 |
| A | ASP287 |
| A | LYS321 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 6051 |
| Chain | Residue |
| A | ARG338 |
| A | PRO339 |
| A | ARG341 |
| A | HOH655 |
| C | ASP177 |
| C | GLN328 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 6201 |
| Chain | Residue |
| A | PRO116 |
| A | ASN209 |
| A | LEU210 |
| A | VAL215 |
| A | PHE243 |
| A | ARG245 |
| A | GLU299 |
| A | GOL6301 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 6301 |
| Chain | Residue |
| A | GLU117 |
| A | ILE118 |
| A | GLY207 |
| A | VAL208 |
| A | PHE243 |
| A | ASP295 |
| A | GOL6201 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 640 |
| Chain | Residue |
| B | GLU271 |
| B | ASP295 |
| B | HOH1195 |
| B | PYR1500 |
| B | HOH1630 |
| site_id | CC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PYR B 1500 |
| Chain | Residue |
| B | ARG72 |
| B | LYS269 |
| B | GLU271 |
| B | ALA292 |
| B | ARG293 |
| B | GLY294 |
| B | ASP295 |
| B | THR327 |
| B | MN640 |
| B | HOH1195 |
| B | HOH1604 |
| B | HOH1630 |
| B | EDO6048 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K B 1700 |
| Chain | Residue |
| B | ASN74 |
| B | SER76 |
| B | ASP112 |
| B | THR113 |
| B | SER242 |
| site_id | CC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA B 2000 |
| Chain | Residue |
| B | SER436 |
| B | HOH1602 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 6007 |
| Chain | Residue |
| B | LYS65 |
| B | SER66 |
| B | HIS378 |
| site_id | CC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 6013 |
| Chain | Residue |
| B | ALA37 |
| B | PRO38 |
| site_id | CC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 6048 |
| Chain | Residue |
| B | ASP177 |
| B | ASP295 |
| B | ILE298 |
| B | HOH1195 |
| B | PYR1500 |
| site_id | CC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 6202 |
| Chain | Residue |
| B | PRO116 |
| B | ASN209 |
| B | LEU210 |
| B | VAL215 |
| B | PHE243 |
| B | ARG245 |
| B | GLU299 |
| site_id | DC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 6302 |
| Chain | Residue |
| B | GLU117 |
| B | ILE118 |
| B | GLY207 |
| B | VAL208 |
| B | PHE243 |
| B | ASP295 |
| B | HOH1232 |
| site_id | DC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 640 |
| Chain | Residue |
| C | GLU271 |
| C | ASP295 |
| C | HOH1196 |
| C | PYR1500 |
| C | HOH1614 |
| site_id | DC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR C 1500 |
| Chain | Residue |
| C | LYS269 |
| C | GLU271 |
| C | ALA292 |
| C | ARG293 |
| C | GLY294 |
| C | ASP295 |
| C | THR327 |
| C | MN640 |
| C | HOH1614 |
| site_id | DC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 1700 |
| Chain | Residue |
| C | ASN74 |
| C | SER76 |
| C | ASP112 |
| C | THR113 |
| C | SER242 |
| C | HOH1097 |
| site_id | DC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA C 2000 |
| Chain | Residue |
| C | THR431 |
| C | SER433 |
| C | SER436 |
| C | HOH1263 |
| site_id | DC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO C 6014 |
| Chain | Residue |
| C | ALA37 |
| C | PRO38 |
| C | THR40 |
| site_id | DC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 6055 |
| Chain | Residue |
| C | PHE97 |
| C | LEU103 |
| C | ARG105 |
| C | ARG499 |
| site_id | DC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL C 6303 |
| Chain | Residue |
| C | GLU117 |
| C | ILE118 |
| C | GLY207 |
| C | VAL208 |
| C | PHE243 |
| C | ASP295 |
| site_id | DC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 6056 |
| Chain | Residue |
| C | ARG391 |
| D | ALA398 |
| D | ARG399 |
| D | SER402 |
| D | HOH1038 |
| D | HOH1610 |
| site_id | EC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN D 640 |
| Chain | Residue |
| D | GLU271 |
| D | ASP295 |
| D | HOH1274 |
| D | PYR1500 |
| site_id | EC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PYR D 1500 |
| Chain | Residue |
| D | LYS269 |
| D | GLU271 |
| D | ALA292 |
| D | ARG293 |
| D | GLY294 |
| D | ASP295 |
| D | THR327 |
| D | MN640 |
| D | HOH1274 |
| D | HOH1625 |
| D | EDO6033 |
| site_id | EC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K D 1700 |
| Chain | Residue |
| D | ASN74 |
| D | SER76 |
| D | ASP112 |
| D | THR113 |
| D | SER242 |
| site_id | EC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 2000 |
| Chain | Residue |
| D | LYS124 |
| D | GLY125 |
| D | THR128 |
| D | HOH1394 |
| site_id | EC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA D 2100 |
| Chain | Residue |
| D | THR431 |
| D | SER433 |
| D | SER436 |
| D | HOH1395 |
| site_id | EC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO D 6011 |
| Chain | Residue |
| D | PRO38 |
| D | THR40 |
| site_id | EC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO D 6017 |
| Chain | Residue |
| D | THR49 |
| D | ARG72 |
| D | ASN74 |
| D | ALA365 |
| site_id | EC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO D 6033 |
| Chain | Residue |
| D | ASP177 |
| D | PYR1500 |
| site_id | EC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 6204 |
| Chain | Residue |
| D | PRO116 |
| D | ASN209 |
| D | LEU210 |
| D | VAL215 |
| D | ARG245 |
| D | GLU299 |
| site_id | FC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 6304 |
| Chain | Residue |
| D | GLU117 |
| D | ILE118 |
| D | VAL208 |
| D | PHE243 |
| D | ASP295 |
| site_id | FC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MN E 640 |
| Chain | Residue |
| E | GLU271 |
| E | ASP295 |
| E | PYR1500 |
| E | HOH1638 |
| site_id | FC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PYR E 1500 |
| Chain | Residue |
| E | LYS269 |
| E | GLU271 |
| E | ALA292 |
| E | ARG293 |
| E | GLY294 |
| E | ASP295 |
| E | THR327 |
| E | MN640 |
| E | HOH1638 |
| site_id | FC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K E 1700 |
| Chain | Residue |
| E | ASN74 |
| E | SER76 |
| E | ASP112 |
| E | THR113 |
| E | HOH1051 |
| site_id | FC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA E 2000 |
| Chain | Residue |
| E | LYS124 |
| E | GLY125 |
| E | SER126 |
| E | GLY127 |
| E | THR128 |
| site_id | FC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA E 2100 |
| Chain | Residue |
| E | THR431 |
| E | SER433 |
| E | SER436 |
| E | HOH1310 |
| E | HOH1396 |
| site_id | FC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO E 6015 |
| Chain | Residue |
| E | PRO38 |
| site_id | FC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO E 6039 |
| Chain | Residue |
| E | ASP177 |
| E | GLY294 |
| E | HOH565 |
| site_id | FC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO E 6046 |
| Chain | Residue |
| E | ILE50 |
| E | GLY51 |
| E | PRO52 |
| E | ASN74 |
| E | ALA365 |
| E | HOH1198 |
| site_id | GC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO E 6049 |
| Chain | Residue |
| E | ARG254 |
| E | GLU284 |
| E | ALA285 |
| E | ASP287 |
| E | LYS321 |
| site_id | GC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL E 6205 |
| Chain | Residue |
| E | PRO116 |
| E | ASN209 |
| E | LEU210 |
| E | VAL215 |
| E | ARG245 |
| E | GLU299 |
| site_id | GC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL E 6305 |
| Chain | Residue |
| E | GLU117 |
| E | ILE118 |
| E | VAL208 |
| E | PHE243 |
| E | ASP295 |
| site_id | GC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN F 640 |
| Chain | Residue |
| F | GLU271 |
| F | ASP295 |
| F | HOH1199 |
| F | PYR1500 |
| F | HOH1624 |
| site_id | GC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PYR F 1500 |
| Chain | Residue |
| F | LYS269 |
| F | GLU271 |
| F | ALA292 |
| F | ARG293 |
| F | GLY294 |
| F | ASP295 |
| F | THR327 |
| F | MN640 |
| F | HOH668 |
| F | HOH1199 |
| site_id | GC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K F 1700 |
| Chain | Residue |
| F | ASN74 |
| F | SER76 |
| F | ASP112 |
| F | THR113 |
| F | SER242 |
| F | HOH1656 |
| site_id | GC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA F 2000 |
| Chain | Residue |
| F | THR431 |
| F | SER433 |
| F | SER436 |
| F | HOH1339 |
| site_id | GC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL F 6010 |
| Chain | Residue |
| F | ASP177 |
| F | GLN328 |
| F | HOH572 |
| F | HOH744 |
| H | ARG338 |
| H | PRO339 |
| H | THR340 |
| H | ARG341 |
| site_id | GC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO F 6012 |
| Chain | Residue |
| F | ALA37 |
| F | PRO38 |
| F | THR40 |
| F | ARG382 |
| site_id | HC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL F 6206 |
| Chain | Residue |
| F | PRO116 |
| F | VAL208 |
| F | ASN209 |
| F | LEU210 |
| F | VAL215 |
| F | PHE243 |
| F | ARG245 |
| F | GLU299 |
| site_id | HC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL F 6306 |
| Chain | Residue |
| F | GLU117 |
| F | ILE118 |
| F | GLY207 |
| F | VAL208 |
| F | PHE243 |
| F | ASP295 |
| F | HOH1624 |
| site_id | HC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN G 640 |
| Chain | Residue |
| G | GLU271 |
| G | ASP295 |
| G | HOH1201 |
| G | HOH1408 |
| G | PYR1500 |
| site_id | HC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PYR G 1500 |
| Chain | Residue |
| G | LYS269 |
| G | GLU271 |
| G | ALA292 |
| G | ARG293 |
| G | GLY294 |
| G | ASP295 |
| G | THR327 |
| G | MN640 |
| G | HOH651 |
| G | HOH1408 |
| site_id | HC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K G 1700 |
| Chain | Residue |
| G | ASN74 |
| G | SER76 |
| G | ASP112 |
| G | THR113 |
| G | SER242 |
| G | HOH651 |
| G | HOH1409 |
| site_id | HC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA G 2000 |
| Chain | Residue |
| G | THR431 |
| G | SER436 |
| site_id | HC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL G 6207 |
| Chain | Residue |
| G | PRO116 |
| G | ASN209 |
| G | LEU210 |
| G | VAL215 |
| G | PHE243 |
| G | ARG245 |
| G | GLU299 |
| G | GOL6307 |
| site_id | HC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL G 6307 |
| Chain | Residue |
| G | GLU117 |
| G | ILE118 |
| G | GLY207 |
| G | VAL208 |
| G | PHE243 |
| G | ASP295 |
| G | HOH1201 |
| G | GOL6207 |
| site_id | HC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN H 640 |
| Chain | Residue |
| H | GLU271 |
| H | ASP295 |
| H | HOH1202 |
| H | PYR1500 |
| H | HOH1607 |
| site_id | IC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PYR H 1500 |
| Chain | Residue |
| H | LYS269 |
| H | GLU271 |
| H | ALA292 |
| H | ARG293 |
| H | GLY294 |
| H | ASP295 |
| H | THR327 |
| H | MN640 |
| H | HOH1202 |
| H | HOH1607 |
| site_id | IC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K H 1700 |
| Chain | Residue |
| H | ASN74 |
| H | SER76 |
| H | ASP112 |
| H | THR113 |
| H | HOH1064 |
| H | HOH1418 |
| site_id | IC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA H 2000 |
| Chain | Residue |
| H | LYS124 |
| H | GLY125 |
| H | SER126 |
| H | GLY127 |
| H | THR128 |
| site_id | IC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA H 2100 |
| Chain | Residue |
| H | THR431 |
| H | SER433 |
| H | SER436 |
| H | HOH1397 |
| site_id | IC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO H 6037 |
| Chain | Residue |
| H | GLU284 |
| H | ALA285 |
| H | SER286 |
| H | ASP287 |
| H | LYS321 |
| site_id | IC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL H 6308 |
| Chain | Residue |
| H | GLU117 |
| H | ILE118 |
| H | GLY207 |
| H | VAL208 |
| H | PHE243 |
| H | ASP295 |
| H | HOH1202 |
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 | 1792 |
| Details | Region: {"description":"Interaction with POU5F1","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 200 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P30613","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 24 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11980","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 8 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 24 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 8 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 16 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
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 |
| site_id | MCSA5 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| E | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| E | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| E | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| E | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA6 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| F | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| F | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| F | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| F | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA7 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| G | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| G | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| G | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| G | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |
| site_id | MCSA8 |
| Number of Residues | 4 |
| Details | M-CSA 326 |
| Chain | Residue | Details |
| H | ARG72 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| H | ARG119 | attractive charge-charge interaction, electrostatic stabiliser, steric role |
| H | LYS269 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role |
| H | THR327 | electrostatic stabiliser, hydrogen bond donor, increase acidity |






