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 | 4 |
Details | BINDING SITE FOR RESIDUE MG A 1432 |
Chain | Residue |
A | GLN162 |
A | ASP241 |
A | GLU287 |
A | LYS390 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 1432 |
Chain | Residue |
B | ASP241 |
B | GLU287 |
B | ASP288 |
B | ASP314 |
B | HOH2084 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 1001 |
Chain | Residue |
B | GLY39 |
B | ALA40 |
B | LYS339 |
B | ARG368 |
B | SER369 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
Chain | Residue |
A | LYS339 |
A | ARG368 |
A | SER369 |
A | HOH2032 |
A | HOH2087 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 2001 |
Chain | Residue |
A | ASP411 |
A | HOH2057 |
B | TYR7 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL A 2002 |
Chain | Residue |
A | ASP5 |
A | TYR7 |
A | TYR25 |
A | HOH2070 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE GOL A 2003 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 2004 |
Chain | Residue |
B | ALA77 |
B | ILE79 |
B | TYR81 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 2005 |
Chain | Residue |
A | MET87 |
A | GLU348 |
A | GLU351 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 2006 |
Chain | Residue |
A | LEU125 |
A | HIS131 |
A | TYR132 |
A | HOH2084 |
B | LEU125 |
B | HIS131 |
B | GLY135 |
B | HOH2083 |
Functional Information from PROSITE/UniProt
site_id | PS00164 |
Number of Residues | 14 |
Details | ENOLASE Enolase signature. ILIKvNQIGTLTET |
Chain | Residue | Details |
A | ILE336-THR349 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | GLU204 | |
B | GLU204 | |
Chain | Residue | Details |
A | LYS339 | |
B | LYS339 | |
Chain | Residue | Details |
A | HIS154 | |
B | ASP314 | |
B | SER366 | |
B | LYS390 | |
A | GLU163 | |
A | GLU287 | |
A | ASP314 | |
A | SER366 | |
A | LYS390 | |
B | HIS154 | |
B | GLU163 | |
B | GLU287 | |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: |
Chain | Residue | Details |
A | ASP241 | |
B | ASP241 | |
Chain | Residue | Details |
A | LYS339 | |
B | LYS339 | |