2FYM
Crystal structure of E. coli enolase complexed with the minimal binding segment of RNase E.
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 | 0005829 | cellular_component | cytosol |
| A | 0005856 | cellular_component | cytoskeleton |
| A | 0006096 | biological_process | glycolytic process |
| A | 0006396 | biological_process | RNA processing |
| A | 0006401 | biological_process | RNA catabolic process |
| A | 0009986 | cellular_component | cell surface |
| A | 0016020 | cellular_component | membrane |
| A | 0016829 | molecular_function | lyase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 1990061 | cellular_component | bacterial degradosome |
| 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 | 0005829 | cellular_component | cytosol |
| C | 0005856 | cellular_component | cytoskeleton |
| C | 0006096 | biological_process | glycolytic process |
| C | 0006396 | biological_process | RNA processing |
| C | 0006401 | biological_process | RNA catabolic process |
| C | 0009986 | cellular_component | cell surface |
| C | 0016020 | cellular_component | membrane |
| C | 0016829 | molecular_function | lyase activity |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 1990061 | cellular_component | bacterial degradosome |
| 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 | 0005829 | cellular_component | cytosol |
| D | 0005856 | cellular_component | cytoskeleton |
| D | 0006096 | biological_process | glycolytic process |
| D | 0006396 | biological_process | RNA processing |
| D | 0006401 | biological_process | RNA catabolic process |
| D | 0009986 | cellular_component | cell surface |
| D | 0016020 | cellular_component | membrane |
| D | 0016829 | molecular_function | lyase activity |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046872 | molecular_function | metal ion binding |
| D | 1990061 | cellular_component | bacterial degradosome |
| F | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| F | 0005515 | molecular_function | protein binding |
| F | 0005576 | cellular_component | extracellular region |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0005829 | cellular_component | cytosol |
| F | 0005856 | cellular_component | cytoskeleton |
| F | 0006096 | biological_process | glycolytic process |
| F | 0006396 | biological_process | RNA processing |
| F | 0006401 | biological_process | RNA catabolic process |
| F | 0009986 | cellular_component | cell surface |
| F | 0016020 | cellular_component | membrane |
| F | 0016829 | molecular_function | lyase activity |
| F | 0042802 | molecular_function | identical protein binding |
| F | 0042803 | molecular_function | protein homodimerization activity |
| F | 0046872 | molecular_function | metal ion binding |
| F | 1990061 | cellular_component | bacterial degradosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1431 |
| Chain | Residue |
| A | ASP245 |
| A | GLU289 |
| A | ASP316 |
| A | HOH1442 |
| A | HOH1729 |
| A | HOH1863 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 1431 |
| Chain | Residue |
| C | HOH1445 |
| C | HOH1835 |
| C | ASP245 |
| C | GLU289 |
| C | ASP316 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 1431 |
| Chain | Residue |
| D | ASP245 |
| D | GLU289 |
| D | ASP316 |
| D | HOH1475 |
| D | HOH1868 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG F 1431 |
| Chain | Residue |
| F | ASP245 |
| F | GLU289 |
| F | ASP316 |
| F | HOH1478 |
| F | HOH1569 |
| F | HOH1573 |
Functional Information from PROSITE/UniProt
| site_id | PS00164 |
| Number of Residues | 14 |
| Details | ENOLASE Enolase signature. ILIKfNQIGSLTET |
| Chain | Residue | Details |
| A | ILE338-THR351 |
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, ECO:0000269|PubMed:15003462 |
| Chain | Residue | Details |
| A | GLY209 | |
| C | GLY209 | |
| D | GLY209 | |
| F | GLY209 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15003462 |
| Chain | Residue | Details |
| A | PHE342 | |
| C | PHE342 | |
| D | PHE342 | |
| F | PHE342 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | SER41 | |
| C | GLY372 | |
| D | SER41 | |
| D | GLU167 | |
| D | PHE342 | |
| D | SER371 | |
| D | GLY372 | |
| F | SER41 | |
| F | GLU167 | |
| F | PHE342 | |
| F | SER371 | |
| A | GLU167 | |
| F | GLY372 | |
| A | PHE342 | |
| A | SER371 | |
| A | GLY372 | |
| C | SER41 | |
| C | GLU167 | |
| C | PHE342 | |
| C | SER371 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30714720, ECO:0007744|PDB:6BFY |
| Chain | Residue | Details |
| A | THR42 | |
| C | THR42 | |
| D | THR42 | |
| F | THR42 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0007744|PDB:6BFY |
| Chain | Residue | Details |
| A | ALA159 | |
| A | GLY209 | |
| C | ALA159 | |
| C | GLY209 | |
| D | ALA159 | |
| D | GLY209 | |
| F | ALA159 | |
| F | GLY209 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0007744|PDB:6BFY, ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | PHE168 | |
| C | PHE168 | |
| D | PHE168 | |
| F | PHE168 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:11676541, ECO:0000269|PubMed:16516921, ECO:0000269|PubMed:20823555, ECO:0007744|PDB:1E9I, ECO:0007744|PDB:2FYM, ECO:0007744|PDB:3H8A, ECO:0007744|PDB:6BFY, ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | CYS246 | |
| C | CYS246 | |
| D | CYS246 | |
| F | CYS246 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:11676541, ECO:0000269|PubMed:20823555, ECO:0000269|PubMed:30714720, ECO:0007744|PDB:1E9I, ECO:0007744|PDB:2FYM, ECO:0007744|PDB:3H8A, ECO:0007744|PDB:6BFY, ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | ASP290 | |
| C | ASP290 | |
| D | ASP290 | |
| F | ASP290 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:11676541, ECO:0000269|PubMed:16516921, ECO:0000269|PubMed:20823555, ECO:0007744|PDB:1E9I, ECO:0007744|PDB:2FYM, ECO:0007744|PDB:6BFY, ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | ASP317 | |
| C | ASP317 | |
| D | ASP317 | |
| F | ASP317 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0007744|PDB:6BFY, ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | THR393 | |
| C | THR393 | |
| D | THR393 | |
| F | THR393 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 12 |
| Details | SITE: Interaction with RNase E => ECO:0000269|PubMed:16516921, ECO:0000269|PubMed:20823555 |
| Chain | Residue | Details |
| A | ALA120 | |
| F | ALA120 | |
| F | ASP376 | |
| F | LEU408 | |
| A | ASP376 | |
| A | LEU408 | |
| C | ALA120 | |
| C | ASP376 | |
| C | LEU408 | |
| D | ALA120 | |
| D | ASP376 | |
| D | LEU408 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | TYR257 | |
| C | TYR257 | |
| D | TYR257 | |
| F | TYR257 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:31328167 |
| Chain | Residue | Details |
| A | PHE342 | |
| C | PHE342 | |
| D | PHE342 | |
| F | PHE342 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | LYS392 | |
| A | GLU208 | |
| A | HIS369 | |
| A | GLU167 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| C | HIS191 | |
| C | LYS341 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| D | HIS191 | |
| D | LYS341 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| F | HIS191 | |
| F | LYS341 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| C | LYS392 | |
| C | GLU208 | |
| C | HIS369 | |
| C | GLU167 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| D | LYS392 | |
| D | GLU208 | |
| D | HIS369 | |
| D | GLU167 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| F | LYS392 | |
| F | GLU208 | |
| F | HIS369 | |
| F | GLU167 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | GLU208 | |
| A | GLU167 | |
| A | HIS369 | |
| A | LYS341 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| C | GLU208 | |
| C | GLU167 | |
| C | HIS369 | |
| C | LYS341 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| D | GLU208 | |
| D | GLU167 | |
| D | HIS369 | |
| D | LYS341 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| F | GLU208 | |
| F | GLU167 | |
| F | HIS369 | |
| F | LYS341 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | HIS191 | |
| A | LYS341 |
