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 | 18 |
| Details | binding site for residue 2PG A 501 |
| Chain | Residue |
| A | GLY39 |
| A | ASP311 |
| A | LEU334 |
| A | LYS336 |
| A | HIS364 |
| A | ARG365 |
| A | SER366 |
| A | LYS387 |
| A | MG502 |
| A | MG503 |
| A | ALA40 |
| A | SER41 |
| A | HIS154 |
| A | GLN162 |
| A | GLU163 |
| A | GLU204 |
| A | ASP241 |
| A | GLU284 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | ASP241 |
| A | GLU284 |
| A | ASP311 |
| A | LYS387 |
| A | 2PG501 |
| A | HOH636 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 503 |
| Chain | Residue |
| A | SER41 |
| A | LYS336 |
| A | 2PG501 |
| A | HOH601 |
| A | HOH840 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | GLN135 |
| A | ASP137 |
| A | ARG347 |
| A | HOH609 |
| A | HOH722 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | GLN179 |
| A | PHE230 |
| A | HOH605 |
| A | HOH608 |
| B | LYS56 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | ARG119 |
| A | LEU129 |
| A | GLN402 |
| A | EDO507 |
| A | HOH649 |
| A | HOH806 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 507 |
| Chain | Residue |
| A | LEU129 |
| A | TYR130 |
| A | ASP376 |
| A | GLN402 |
| A | EDO506 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| B | GLN135 |
| B | ASP137 |
| B | ARG347 |
| B | HOH614 |
| B | HOH829 |
| site_id | AC9 |
| Number of Residues | 18 |
| Details | binding site for residue 2PG B 502 |
| Chain | Residue |
| B | GLY39 |
| B | ALA40 |
| B | SER41 |
| B | HIS154 |
| B | GLN162 |
| B | GLU163 |
| B | GLU204 |
| B | ASP241 |
| B | GLU284 |
| B | ASP311 |
| B | LEU334 |
| B | LYS336 |
| B | HIS364 |
| B | ARG365 |
| B | SER366 |
| B | LYS387 |
| B | MG503 |
| B | MG504 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 503 |
| Chain | Residue |
| B | ASP241 |
| B | GLU284 |
| B | ASP311 |
| B | LYS387 |
| B | 2PG502 |
| B | HOH676 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 504 |
| Chain | Residue |
| B | SER41 |
| B | LYS336 |
| B | 2PG502 |
| B | HOH603 |
| B | HOH863 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 505 |
| Chain | Residue |
| A | LYS56 |
| B | GLN179 |
| B | PHE230 |
| B | HOH675 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 506 |
| Chain | Residue |
| B | LEU129 |
| B | ASP376 |
| B | GLN402 |
| B | HOH647 |
| B | HOH857 |
Functional Information from PROSITE/UniProt
| site_id | PS00164 |
| Number of Residues | 14 |
| Details | ENOLASE Enolase signature. ILIKvNQIGTLSET |
| Chain | Residue | Details |
| A | ILE333-THR346 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"6NB2","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"6NB2","evidenceCode":"ECO:0007744"}]} |
