3TQP
Structure of an enolase (eno) from Coxiella burnetii
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 | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 429 |
| Chain | Residue |
| B | LYS337 |
| B | ARG366 |
| B | SER367 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 429 |
| Chain | Residue |
| A | HOH558 |
| A | GLY41 |
| A | ALA42 |
| A | LYS337 |
| A | ARG366 |
| A | SER367 |
| A | HOH556 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 430 |
| Chain | Residue |
| B | ASP244 |
| B | GLU285 |
| B | ASP312 |
| B | HOH464 |
| B | HOH480 |
| B | HOH495 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 430 |
| Chain | Residue |
| A | ASP244 |
| A | GLU285 |
| A | ASP312 |
| A | HOH549 |
| A | HOH556 |
| A | HOH558 |
Functional Information from PROSITE/UniProt
| site_id | PS00164 |
| Number of Residues | 14 |
| Details | ENOLASE Enolase signature. ILVKlNQIGTLTET |
| Chain | Residue | Details |
| A | ILE334-THR347 |
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"}]} |
| Chain | Residue | Details |
| 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26033498","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3TQP","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
