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 | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006096 | biological_process | glycolytic process |
| 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 | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006096 | biological_process | glycolytic process |
| 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 2PG A 437 |
| Chain | Residue |
| A | GLN164 |
| A | HOH683 |
| A | HOH730 |
| A | HOH794 |
| A | HOH1110 |
| A | GLU208 |
| A | ASP322 |
| A | LYS347 |
| A | HIS375 |
| A | ARG376 |
| A | SER377 |
| A | MG441 |
| A | HOH559 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 438 |
| Chain | Residue |
| A | ALA39 |
| A | SER40 |
| A | THR41 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 439 |
| Chain | Residue |
| A | PRO127 |
| A | TYR129 |
| A | GLN413 |
| A | GLU420 |
| A | HOH495 |
| A | HOH668 |
| A | HOH701 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 440 |
| Chain | Residue |
| A | HIS177 |
| A | GLU178 |
| A | ARG181 |
| A | HOH618 |
| B | ARG56 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 441 |
| Chain | Residue |
| A | ASP243 |
| A | GLU296 |
| A | ASP322 |
| A | 2PG437 |
| A | HOH680 |
| A | HOH683 |
| site_id | AC6 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 2PG B 437 |
| Chain | Residue |
| B | GLY38 |
| B | ALA39 |
| B | SER40 |
| B | GLN164 |
| B | GLU165 |
| B | GLU208 |
| B | ASP243 |
| B | GLU296 |
| B | ASP322 |
| B | LYS347 |
| B | HIS375 |
| B | ARG376 |
| B | SER377 |
| B | LYS398 |
| B | MG441 |
| B | HOH527 |
| B | HOH678 |
| B | HOH812 |
| B | HOH828 |
| B | HOH830 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 438 |
| Chain | Residue |
| B | HIS44 |
| B | ASN328 |
| B | HOH488 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 439 |
| Chain | Residue |
| B | HIS289 |
| B | GLN333 |
| B | ASP337 |
| B | LYS367 |
| B | HOH475 |
| B | HOH672 |
| B | HOH800 |
| B | HOH918 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 440 |
| Chain | Residue |
| A | ARG56 |
| B | HIS177 |
| B | GLU178 |
| B | ARG181 |
| B | HOH700 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 441 |
| Chain | Residue |
| B | ASP243 |
| B | GLU296 |
| B | ASP322 |
| B | 2PG437 |
| B | HOH669 |
Functional Information from PROSITE/UniProt
| site_id | PS00164 |
| Number of Residues | 14 |
| Details | ENOLASE Enolase signature. VLIKvNQIGTLTET |
| Chain | Residue | Details |
| A | VAL344-THR357 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | GLU208 | |
| B | GLU208 | |
| Chain | Residue | Details |
| A | LYS347 | |
| B | LYS347 | |
| Chain | Residue | Details |
| A | SER40 | |
| B | SER40 | |
| Chain | Residue | Details |
| A | GLN164 | |
| A | GLU208 | |
| A | ASP243 | |
| A | GLU296 | |
| A | ASP322 | |
| A | ARG376 | |
| A | SER377 | |
| B | GLN164 | |
| B | GLU208 | |
| B | ASP243 | |
| B | GLU296 | |
| B | ASP322 | |
| B | ARG376 | |
| B | SER377 | |
