Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004743 | molecular_function | pyruvate kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006096 | biological_process | glycolytic process |
| 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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004743 | molecular_function | pyruvate kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006096 | biological_process | glycolytic process |
| 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 |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004743 | molecular_function | pyruvate kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0005886 | cellular_component | plasma membrane |
| C | 0006096 | biological_process | glycolytic process |
| 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 |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004743 | molecular_function | pyruvate kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0006096 | biological_process | glycolytic process |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 501 |
| Chain | Residue |
| A | GLU220 |
| A | ASP244 |
| A | OXL502 |
| A | HOH602 |
| A | HOH607 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue OXL A 502 |
| Chain | Residue |
| A | GLY243 |
| A | ASP244 |
| A | THR276 |
| A | MG501 |
| A | HOH602 |
| A | HOH604 |
| A | HOH607 |
| A | LYS218 |
| A | GLU220 |
| A | ALA241 |
| A | ARG242 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | binding site for residue R5P A 503 |
| Chain | Residue |
| A | GLU267 |
| A | ASN268 |
| A | HIS345 |
| A | PRO347 |
| A | ARG348 |
| A | THR349 |
| A | GLY352 |
| A | ARG382 |
| A | ARG385 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | binding site for residue AMP A 504 |
| Chain | Residue |
| A | ARG351 |
| A | PHE373 |
| A | THR374 |
| A | GLN375 |
| A | SER376 |
| A | THR379 |
| A | ALA397 |
| A | VAL416 |
| A | PRO417 |
| A | LYS418 |
| A | MET419 |
| A | MET425 |
| A | GLY450 |
| A | PRO453 |
| A | GLY454 |
| A | THR455 |
| A | VAL456 |
| A | GLY457 |
| A | SER458 |
| A | THR459 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 501 |
| Chain | Residue |
| B | LYS218 |
| B | GLU220 |
| B | ASP244 |
| B | OXL502 |
| B | HOH603 |
| B | HOH633 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue OXL B 502 |
| Chain | Residue |
| B | LYS218 |
| B | GLU220 |
| B | ALA241 |
| B | ARG242 |
| B | GLY243 |
| B | ASP244 |
| B | THR276 |
| B | MG501 |
| B | HOH633 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | binding site for residue R5P B 503 |
| Chain | Residue |
| B | GLU267 |
| B | ASN268 |
| B | HIS345 |
| B | PRO347 |
| B | ARG348 |
| B | THR349 |
| B | GLY352 |
| B | ARG382 |
| B | ARG385 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | binding site for residue AMP B 504 |
| Chain | Residue |
| B | ARG351 |
| B | PHE373 |
| B | THR374 |
| B | GLN375 |
| B | SER376 |
| B | THR379 |
| B | ALA397 |
| B | VAL416 |
| B | PRO417 |
| B | LYS418 |
| B | MET419 |
| B | MET425 |
| B | GLY450 |
| B | PRO453 |
| B | GLY454 |
| B | THR455 |
| B | GLY457 |
| B | SER458 |
| B | THR459 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 501 |
| Chain | Residue |
| C | GLU220 |
| C | ASP244 |
| C | OXL502 |
| C | HOH607 |
| C | HOH612 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue OXL C 502 |
| Chain | Residue |
| C | THR276 |
| C | MG501 |
| C | LYS218 |
| C | GLU220 |
| C | ALA241 |
| C | ARG242 |
| C | GLY243 |
| C | ASP244 |
| site_id | AD2 |
| Number of Residues | 9 |
| Details | binding site for residue R5P C 503 |
| Chain | Residue |
| C | GLU267 |
| C | ASN268 |
| C | HIS345 |
| C | PRO347 |
| C | ARG348 |
| C | THR349 |
| C | GLY352 |
| C | ARG382 |
| C | ARG385 |
| site_id | AD3 |
| Number of Residues | 20 |
| Details | binding site for residue AMP C 504 |
| Chain | Residue |
| C | ARG351 |
| C | PHE373 |
| C | THR374 |
| C | GLN375 |
| C | SER376 |
| C | THR379 |
| C | ALA397 |
| C | VAL416 |
| C | PRO417 |
| C | LYS418 |
| C | MET419 |
| C | MET425 |
| C | GLY450 |
| C | PRO453 |
| C | GLY454 |
| C | THR455 |
| C | VAL456 |
| C | GLY457 |
| C | SER458 |
| C | THR459 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue MG D 501 |
| Chain | Residue |
| D | LYS218 |
| D | GLU220 |
| D | ASP244 |
| D | OXL502 |
| D | HOH602 |
| D | HOH607 |
| site_id | AD5 |
| Number of Residues | 9 |
| Details | binding site for residue OXL D 502 |
| Chain | Residue |
| D | LYS218 |
| D | GLU220 |
| D | ALA241 |
| D | ARG242 |
| D | GLY243 |
| D | ASP244 |
| D | THR276 |
| D | MG501 |
| D | HOH602 |
| site_id | AD6 |
| Number of Residues | 10 |
| Details | binding site for residue R5P D 503 |
| Chain | Residue |
| D | GLU267 |
| D | ASN268 |
| D | HIS345 |
| D | PRO347 |
| D | ARG348 |
| D | THR349 |
| D | GLY352 |
| D | ARG382 |
| D | ARG385 |
| D | HOH615 |
| site_id | AD7 |
| Number of Residues | 20 |
| Details | binding site for residue AMP D 504 |
| Chain | Residue |
| D | ARG351 |
| D | PHE373 |
| D | THR374 |
| D | GLN375 |
| D | SER376 |
| D | THR379 |
| D | PHE395 |
| D | ALA397 |
| D | VAL416 |
| D | PRO417 |
| D | LYS418 |
| D | MET419 |
| D | MET425 |
| D | GLY450 |
| D | GLY454 |
| D | THR455 |
| D | VAL456 |
| D | GLY457 |
| D | SER458 |
| D | THR459 |
Functional Information from PROSITE/UniProt
| site_id | PS00110 |
| Number of Residues | 13 |
| Details | PYRUVATE_KINASE Pyruvate kinase active site signature. VpVIAKLEKpEAI |
| Chain | Residue | Details |
| A | VAL213-ILE225 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine; by PknJ; in vitro","evidences":[{"source":"PubMed","id":"20520732","evidenceCode":"ECO:0000269"}]} |
