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 | 0005737 | cellular_component | cytoplasm |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PGA A 439 |
| Chain | Residue |
| A | SER36 |
| A | HIS157 |
| A | GLU209 |
| A | LYS344 |
| A | ARG373 |
| A | SER374 |
| A | HOH441 |
| A | HOH444 |
| A | HOH569 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MN A 440 |
| Chain | Residue |
| A | ASP244 |
| A | GLU294 |
| A | ASP319 |
| A | HOH441 |
| A | HOH442 |
| A | HOH443 |
Functional Information from PROSITE/UniProt
| site_id | PS00164 |
| Number of Residues | 14 |
| Details | ENOLASE Enolase signature. LLLKvNQIGSVTES |
| Chain | Residue | Details |
| A | LEU341-SER354 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 5 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7547999","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1PDZ","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7547999","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1PDZ","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"7547999","evidenceCode":"ECO:0000305"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | LYS395 | |
| A | HIS372 | |
| A | GLU209 | |
| A | GLU166 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | HIS372 | |
| A | GLU209 | |
| A | GLU166 | |
| A | LYS344 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | HIS189 | |
| A | LYS344 | |
