4A3R
Crystal structure of Enolase from Bacillus subtilis.
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 | 0005515 | molecular_function | protein binding |
| 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 | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| 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 | 0005515 | molecular_function | protein binding |
| 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 | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005576 | cellular_component | extracellular region |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006096 | biological_process | glycolytic process |
| C | 0009986 | cellular_component | cell surface |
| C | 0016829 | molecular_function | lyase activity |
| C | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005576 | cellular_component | extracellular region |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006096 | biological_process | glycolytic process |
| D | 0009986 | cellular_component | cell surface |
| D | 0016829 | molecular_function | lyase activity |
| D | 0030435 | biological_process | sporulation resulting in formation of a cellular spore |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE CIT D 1429 |
| Chain | Residue |
| D | GLY40 |
| D | SER369 |
| D | LYS390 |
| D | NA1430 |
| D | NA1431 |
| D | HOH2112 |
| D | ALA41 |
| D | SER42 |
| D | GLN163 |
| D | GLU164 |
| D | GLU205 |
| D | LYS339 |
| D | HIS367 |
| D | ARG368 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA D 1430 |
| Chain | Residue |
| D | ASP242 |
| D | GLU287 |
| D | ASP314 |
| D | CIT1429 |
| D | HOH2138 |
| D | HOH2161 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA D 1431 |
| Chain | Residue |
| D | SER42 |
| D | CIT1429 |
| D | HOH2033 |
| D | HOH2040 |
| D | HOH2161 |
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
| site_id | SWS_FT_FI1 |
| Number of Residues | 556 |
| Details | Region: {"description":"Sufficient for secretion","evidences":[{"source":"PubMed","id":"24642254","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17218307","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17218307","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"17218307","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
