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 | 0006096 | biological_process | glycolytic process |
| A | 0006950 | biological_process | response to stress |
| 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 |
| 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 | 0006096 | biological_process | glycolytic process |
| D | 0006950 | biological_process | response to stress |
| 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 | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 499 |
| Chain | Residue |
| D | SER53 |
| D | THR84 |
| D | LYS85 |
| D | SER211 |
| D | LYS238 |
| D | GLU240 |
| D | K503 |
| D | HOH782 |
| D | HOH873 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 500 |
| Chain | Residue |
| D | ASP232 |
| D | ARG424 |
| D | GLN426 |
| D | THR427 |
| D | GLN430 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 D 501 |
| Chain | Residue |
| D | SER400 |
| D | ASN401 |
| D | THR402 |
| D | ARG404 |
| D | SER405 |
| D | ASP482 |
| D | HIS483 |
| D | HOH619 |
| D | HOH724 |
| D | HOH801 |
| D | HOH883 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE K D 502 |
| Chain | Residue |
| D | GLN354 |
| D | LEU357 |
| D | GLU359 |
| D | HOH872 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE K D 503 |
| Chain | Residue |
| D | ASN51 |
| D | SER53 |
| D | ASP83 |
| D | THR84 |
| D | LYS238 |
| D | GOL499 |
| D | HOH873 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 499 |
| Chain | Residue |
| A | GLU438 |
| A | SER439 |
| A | PHE463 |
| A | HOH667 |
| A | HOH724 |
| A | HOH732 |
| A | HOH734 |
| A | HOH746 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 500 |
| Chain | Residue |
| A | SER400 |
| A | ASN401 |
| A | THR402 |
| A | ARG404 |
| A | SER405 |
| A | HOH815 |
| A | HOH830 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 501 |
| Chain | Residue |
| A | GLN354 |
| A | LEU357 |
| A | GLU359 |
| A | HOH681 |
| A | HOH797 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 502 |
| Chain | Residue |
| A | ASN51 |
| A | SER53 |
| A | ASP83 |
| A | THR84 |
| A | HOH678 |
Functional Information from PROSITE/UniProt
| site_id | PS00110 |
| Number of Residues | 13 |
| Details | PYRUVATE_KINASE Pyruvate kinase active site signature. ImIICKIENhQGV |
| Chain | Residue | Details |
| D | ILE233-VAL245 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer"} |
