Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000015 | cellular_component | phosphopyruvate hydratase complex |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004634 | molecular_function | phosphopyruvate hydratase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0005737 | cellular_component | cytoplasm |
A | 0006096 | biological_process | glycolytic process |
A | 0009986 | cellular_component | cell surface |
A | 0016829 | molecular_function | lyase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000015 | cellular_component | phosphopyruvate hydratase complex |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004634 | molecular_function | phosphopyruvate hydratase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005737 | cellular_component | cytoplasm |
B | 0006096 | biological_process | glycolytic process |
B | 0009986 | cellular_component | cell surface |
B | 0016829 | molecular_function | lyase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | binding site for residue PEP A 501 |
Chain | Residue |
A | GLY40 |
A | LYS394 |
A | MG502 |
A | HOH687 |
A | HOH747 |
A | ALA41 |
A | SER42 |
A | ASP244 |
A | ASP318 |
A | LYS343 |
A | HIS371 |
A | ARG372 |
A | SER373 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue MG A 502 |
Chain | Residue |
A | ASP244 |
A | GLU291 |
A | ASP318 |
A | PEP501 |
A | HOH686 |
A | HOH687 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | TYR133 |
A | GLN409 |
A | GLU416 |
A | HOH684 |
A | HOH710 |
A | HOH733 |
B | ARG34 |
B | HOH651 |
site_id | AC4 |
Number of Residues | 13 |
Details | binding site for residue PEP B 501 |
Chain | Residue |
B | GLY40 |
B | ALA41 |
B | SER42 |
B | ASP244 |
B | ASP318 |
B | LYS343 |
B | HIS371 |
B | ARG372 |
B | SER373 |
B | LYS394 |
B | MG502 |
B | HOH724 |
B | HOH748 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MG B 502 |
Chain | Residue |
B | ASP244 |
B | GLU291 |
B | ASP318 |
B | PEP501 |
B | HOH644 |
B | HOH724 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue GOL B 503 |
Chain | Residue |
A | ARG34 |
A | HOH636 |
B | TYR133 |
B | GLN409 |
B | GLU416 |
B | HOH671 |
B | HOH700 |
B | HOH709 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue GOL B 504 |
Chain | Residue |
A | ASP88 |
A | SER91 |
A | HOH835 |
B | LYS134 |
B | GLU416 |
B | LEU417 |
B | PHE418 |
B | GLU419 |
B | HOH722 |
Functional Information from PROSITE/UniProt
site_id | PS00164 |
Number of Residues | 14 |
Details | ENOLASE Enolase signature. ILIKvNQIGTLTET |
Chain | Residue | Details |
A | ILE340-THR353 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU207 | |
B | GLU207 | |
Chain | Residue | Details |
A | LYS343 | |
B | LYS343 | |
Chain | Residue | Details |
A | HIS157 | |
B | ASP244 | |
B | GLU291 | |
B | ASP318 | |
B | SER370 | |
B | LYS394 | |
A | GLU166 | |
A | ASP244 | |
A | GLU291 | |
A | ASP318 | |
A | SER370 | |
A | LYS394 | |
B | HIS157 | |
B | GLU166 | |
Chain | Residue | Details |
A | LYS343 | |
B | LYS343 | |