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 | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00318 |
| Chain | Residue | Details |
| A | GLU205 | |
| B | GLU205 | |
| C | GLU205 | |
| D | GLU205 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318 |
| Chain | Residue | Details |
| A | LYS339 | |
| B | LYS339 | |
| C | LYS339 | |
| D | LYS339 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318 |
| Chain | Residue | Details |
| A | GLN163 | |
| B | ASP242 | |
| B | GLU287 | |
| B | ASP314 | |
| B | LYS339 | |
| B | ARG368 | |
| B | SER369 | |
| B | LYS390 | |
| C | GLN163 | |
| C | ASP242 | |
| C | GLU287 | |
| A | ASP242 | |
| C | ASP314 | |
| C | LYS339 | |
| C | ARG368 | |
| C | SER369 | |
| C | LYS390 | |
| D | GLN163 | |
| D | ASP242 | |
| D | GLU287 | |
| D | ASP314 | |
| D | LYS339 | |
| A | GLU287 | |
| D | ARG368 | |
| D | SER369 | |
| D | LYS390 | |
| A | ASP314 | |
| A | LYS339 | |
| A | ARG368 | |
| A | SER369 | |
| A | LYS390 | |
| B | GLN163 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:17218307 |
| Chain | Residue | Details |
| A | THR141 | |
| B | THR141 | |
| C | THR141 | |
| D | THR141 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:17218307 |
| Chain | Residue | Details |
| A | SER259 | |
| A | SER325 | |
| B | SER259 | |
| B | SER325 | |
| C | SER259 | |
| C | SER325 | |
| D | SER259 | |
| D | SER325 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000269|PubMed:17218307 |
| Chain | Residue | Details |
| A | TYR281 | |
| B | TYR281 | |
| C | TYR281 | |
| D | TYR281 |
