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 | 0006096 | biological_process | glycolytic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030955 | molecular_function | potassium ion binding |
| A | 0032869 | biological_process | cellular response to insulin stimulus |
| 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 | 0006096 | biological_process | glycolytic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030955 | molecular_function | potassium ion binding |
| B | 0032869 | biological_process | cellular response to insulin stimulus |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 499 |
| Chain | Residue |
| A | SER400 |
| A | ASN401 |
| A | THR402 |
| A | ARG404 |
| A | SER405 |
| A | TYR488 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 500 |
| Chain | Residue |
| A | ILE233 |
| A | ASP256 |
| A | ARG223 |
| A | ARG231 |
| A | ASP232 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PTK A 501 |
| Chain | Residue |
| A | ARG194 |
| A | ARG194 |
| A | LYS224 |
| A | LYS224 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 502 |
| Chain | Residue |
| A | LYS279 |
| A | PHE321 |
| A | ASN322 |
| A | PHE362 |
| A | HOH547 |
| B | LEU3 |
| B | ASN6 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 499 |
| Chain | Residue |
| B | SER330 |
| B | GLY331 |
| B | LYS335 |
| B | HOH743 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | THR26 |
| A | ASN51 |
| A | GLY331 |
| A | LYS335 |
| A | HOH686 |
| A | HOH753 |
Functional Information from PROSITE/UniProt
| site_id | PS00110 |
| Number of Residues | 13 |
| Details | PYRUVATE_KINASE Pyruvate kinase active site signature. ImIICKIENhQGV |
| Chain | Residue | Details |
| A | ILE233-VAL245 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG49 | |
| B | ARG49 | |
| B | ASN51 | |
| B | SER53 | |
| B | ASP83 | |
| B | THR84 | |
| B | GLU240 | |
| B | GLY263 | |
| B | ASP264 | |
| B | THR296 | |
| A | ASN51 | |
| A | SER53 | |
| A | ASP83 | |
| A | THR84 | |
| A | GLU240 | |
| A | GLY263 | |
| A | ASP264 | |
| A | THR296 | |
| Chain | Residue | Details |
| A | ARG90 | |
| B | ARG90 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer |
| Chain | Residue | Details |
| A | LYS238 | |
| B | LYS238 | |
