Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 0016301 | molecular_function | kinase activity |
A | 0030955 | molecular_function | potassium ion binding |
A | 0046872 | molecular_function | metal ion 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 | 0016301 | molecular_function | kinase 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: BINDING => ECO:0000250 |
Chain | Residue | Details |
D | ARG49 | |
A | ARG49 | |
A | ASN51 | |
A | SER53 | |
A | ASP83 | |
A | THR84 | |
A | GLU240 | |
A | GLY263 | |
A | ASP264 | |
A | THR296 | |
D | ASN51 | |
D | SER53 | |
D | ASP83 | |
D | THR84 | |
D | GLU240 | |
D | GLY263 | |
D | ASP264 | |
D | THR296 | |
Chain | Residue | Details |
D | ARG90 | |
A | ARG90 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
D | LYS238 | |
A | LYS238 | |