6D3Q
Crystal structure of Escherichia coli enolase complexed with a natural inhibitor SF2312.
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 |
| 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 | 0005829 | cellular_component | cytosol |
| B | 0005856 | cellular_component | cytoskeleton |
| B | 0006096 | biological_process | glycolytic process |
| B | 0006396 | biological_process | RNA processing |
| B | 0006401 | biological_process | RNA catabolic process |
| B | 0009986 | cellular_component | cell surface |
| B | 0016020 | cellular_component | membrane |
| B | 0016829 | molecular_function | lyase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 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 |
| E | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0005576 | cellular_component | extracellular region |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0005829 | cellular_component | cytosol |
| E | 0005856 | cellular_component | cytoskeleton |
| E | 0006096 | biological_process | glycolytic process |
| E | 0006396 | biological_process | RNA processing |
| E | 0006401 | biological_process | RNA catabolic process |
| E | 0009986 | cellular_component | cell surface |
| E | 0016020 | cellular_component | membrane |
| E | 0016829 | molecular_function | lyase activity |
| E | 0042802 | molecular_function | identical protein binding |
| E | 0042803 | molecular_function | protein homodimerization activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 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 | 19 |
| Details | binding site for residue 4NG A 501 |
| Chain | Residue |
| A | GLY39 |
| A | LEU339 |
| A | LYS341 |
| A | HIS369 |
| A | ARG370 |
| A | SER371 |
| A | LYS392 |
| A | MG502 |
| A | MG503 |
| A | HOH638 |
| A | HOH645 |
| A | ALA40 |
| A | SER41 |
| A | GLN166 |
| A | GLU167 |
| A | GLU208 |
| A | ASP245 |
| A | GLU289 |
| A | ASP316 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | ASP245 |
| A | GLU289 |
| A | ASP316 |
| A | 4NG501 |
| A | HOH627 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 503 |
| Chain | Residue |
| A | SER41 |
| A | 4NG501 |
| A | HOH638 |
| A | HOH645 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | ILE94 |
| A | THR99 |
| A | GLU100 |
| A | LYS102 |
| A | LYS324 |
| A | GLU350 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | binding site for residue 4NG C 501 |
| Chain | Residue |
| C | GLY39 |
| C | ALA40 |
| C | SER41 |
| C | GLN166 |
| C | GLU167 |
| C | GLU208 |
| C | ASP245 |
| C | GLU289 |
| C | ASP316 |
| C | LYS341 |
| C | HIS369 |
| C | ARG370 |
| C | SER371 |
| C | LYS392 |
| C | MG502 |
| C | MG503 |
| C | HOH603 |
| C | HOH616 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue MG C 502 |
| Chain | Residue |
| C | ASP245 |
| C | GLU289 |
| C | ASP316 |
| C | 4NG501 |
| C | HOH609 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | binding site for residue MG C 503 |
| Chain | Residue |
| C | SER41 |
| C | 4NG501 |
| C | HOH603 |
| C | HOH616 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 504 |
| Chain | Residue |
| A | ARG-3 |
| B | ARG-3 |
| C | ARG-3 |
| C | GLY-4 |
| C | HOH601 |
| F | GLN-6 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 505 |
| Chain | Residue |
| C | LYS179 |
| C | GLU180 |
| C | ARG183 |
| D | ARG57 |
| site_id | AD1 |
| Number of Residues | 19 |
| Details | binding site for residue 4NG B 501 |
| Chain | Residue |
| B | GLY39 |
| B | ALA40 |
| B | SER41 |
| B | GLN166 |
| B | GLU167 |
| B | GLU208 |
| B | ASP245 |
| B | GLU289 |
| B | ASP316 |
| B | LEU339 |
| B | LYS341 |
| B | HIS369 |
| B | ARG370 |
| B | SER371 |
| B | LYS392 |
| B | MG502 |
| B | MG503 |
| B | HOH645 |
| B | HOH652 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | ASP245 |
| B | GLU289 |
| B | ASP316 |
| B | 4NG501 |
| B | HOH632 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 503 |
| Chain | Residue |
| B | SER41 |
| B | 4NG501 |
| B | HOH645 |
| B | HOH652 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| B | ILE94 |
| B | THR99 |
| B | GLU100 |
| B | LYS102 |
| B | GLU350 |
| B | HOH612 |
| B | HOH671 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 B 505 |
| Chain | Residue |
| A | GLU180 |
| A | ARG183 |
| B | ARG57 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 B 506 |
| Chain | Residue |
| A | ARG57 |
| B | GLU180 |
| B | ARG183 |
| B | HOH627 |
| site_id | AD7 |
| Number of Residues | 20 |
| Details | binding site for residue 4NG E 501 |
| Chain | Residue |
| E | GLY39 |
| E | ALA40 |
| E | SER41 |
| E | GLN166 |
| E | GLU167 |
| E | GLU208 |
| E | ASP245 |
| E | GLU289 |
| E | ASP316 |
| E | LEU339 |
| E | LYS341 |
| E | HIS369 |
| E | ARG370 |
| E | SER371 |
| E | LYS392 |
| E | MG502 |
| E | MG503 |
| E | HOH607 |
| E | HOH637 |
| E | HOH641 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue MG E 502 |
| Chain | Residue |
| E | ASP245 |
| E | GLU289 |
| E | ASP316 |
| E | 4NG501 |
| E | HOH637 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue MG E 503 |
| Chain | Residue |
| E | SER41 |
| E | 4NG501 |
| E | HOH607 |
| E | HOH641 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue GOL E 504 |
| Chain | Residue |
| E | ILE94 |
| E | THR99 |
| E | GLU100 |
| E | LYS102 |
| E | LYS324 |
| E | GLU350 |
| E | HOH609 |
| site_id | AE2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 E 505 |
| Chain | Residue |
| E | LYS179 |
| E | GLU180 |
| E | ARG183 |
| F | ARG57 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 E 506 |
| Chain | Residue |
| E | THR99 |
| E | GLU100 |
| E | ASN101 |
| E | SER103 |
| site_id | AE4 |
| Number of Residues | 19 |
| Details | binding site for residue 4NG F 501 |
| Chain | Residue |
| F | GLY39 |
| F | ALA40 |
| F | SER41 |
| F | GLN166 |
| F | GLU167 |
| F | GLU208 |
| F | ASP245 |
| F | GLU289 |
| F | ASP316 |
| F | LEU339 |
| F | LYS341 |
| F | HIS369 |
| F | ARG370 |
| F | SER371 |
| F | LYS392 |
| F | MG502 |
| F | MG503 |
| F | HOH614 |
| F | HOH640 |
| site_id | AE5 |
| Number of Residues | 6 |
| Details | binding site for residue MG F 502 |
| Chain | Residue |
| F | ASP245 |
| F | GLU289 |
| F | ASP316 |
| F | LYS392 |
| F | 4NG501 |
| F | HOH637 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for residue MG F 503 |
| Chain | Residue |
| F | SER41 |
| F | 4NG501 |
| F | HOH614 |
| F | HOH640 |
| site_id | AE7 |
| Number of Residues | 5 |
| Details | binding site for residue GOL F 504 |
| Chain | Residue |
| F | ILE94 |
| F | THR99 |
| F | GLU100 |
| F | LYS102 |
| F | GLU350 |
| site_id | AE8 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 F 505 |
| Chain | Residue |
| A | ARG-3 |
| A | GLY-4 |
| D | GLN-6 |
| E | ARG-3 |
| F | ARG-3 |
| F | HOH601 |
| F | HOH607 |
| site_id | AE9 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 F 506 |
| Chain | Residue |
| E | ARG57 |
| F | LYS179 |
| F | GLU180 |
| F | ARG183 |
| site_id | AF1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 F 507 |
| Chain | Residue |
| F | THR99 |
| F | GLU100 |
| F | ASN101 |
| F | SER103 |
| site_id | AF2 |
| Number of Residues | 19 |
| Details | binding site for residue 4NG D 501 |
| Chain | Residue |
| D | GLY39 |
| D | ALA40 |
| D | SER41 |
| D | GLN166 |
| D | GLU167 |
| D | GLU208 |
| D | ASP245 |
| D | GLU289 |
| D | ASP316 |
| D | LEU339 |
| D | LYS341 |
| D | HIS369 |
| D | ARG370 |
| D | SER371 |
| D | LYS392 |
| D | MG502 |
| D | MG503 |
| D | HOH604 |
| D | HOH632 |
| site_id | AF3 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 502 |
| Chain | Residue |
| D | ASP245 |
| D | GLU289 |
| D | ASP316 |
| D | 4NG501 |
| D | HOH610 |
| site_id | AF4 |
| Number of Residues | 4 |
| Details | binding site for residue MG D 503 |
| Chain | Residue |
| D | SER41 |
| D | 4NG501 |
| D | HOH604 |
| D | HOH632 |
| site_id | AF5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 504 |
| Chain | Residue |
| D | ILE94 |
| D | THR99 |
| D | GLU100 |
| D | LYS102 |
| D | GLU350 |
| site_id | AF6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 D 505 |
| Chain | Residue |
| B | GLN-6 |
| C | ARG-3 |
| D | ARG-3 |
| D | HOH601 |
| E | ARG-3 |
| F | ARG-3 |
| site_id | AF7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 D 506 |
| Chain | Residue |
| C | ARG57 |
| D | LYS179 |
| D | GLU180 |
| D | ARG183 |
| D | HOH661 |
| site_id | AF8 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 507 |
| Chain | Residue |
| D | THR99 |
| D | ASN101 |
| D | SER103 |
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 | 6 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15003462 |
| Chain | Residue | Details |
| A | GLU208 | |
| C | GLU208 | |
| B | GLU208 | |
| E | GLU208 | |
| F | GLU208 | |
| D | GLU208 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0000269|PubMed:15003462 |
| Chain | Residue | Details |
| A | LYS341 | |
| C | LYS341 | |
| B | LYS341 | |
| E | LYS341 | |
| F | LYS341 | |
| D | LYS341 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| F | ARG370 | |
| F | SER371 | |
| D | GLN166 | |
| D | LYS341 | |
| D | ARG370 | |
| D | SER371 | |
| A | ALA40 | |
| C | ALA40 | |
| B | ALA40 | |
| E | ALA40 | |
| F | ALA40 | |
| D | ALA40 | |
| C | LYS341 | |
| A | GLN166 | |
| A | LYS341 | |
| A | ARG370 | |
| A | SER371 | |
| C | GLN166 | |
| C | ARG370 | |
| C | SER371 | |
| B | GLN166 | |
| B | LYS341 | |
| B | ARG370 | |
| B | SER371 | |
| E | GLN166 | |
| E | LYS341 | |
| E | ARG370 | |
| E | SER371 | |
| F | GLN166 | |
| F | LYS341 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| 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 |
| C | ASP245 | |
| B | ASP245 | |
| E | ASP245 | |
| F | ASP245 | |
| D | ASP245 | |
| A | ASP245 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| 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 | GLU289 | |
| C | GLU289 | |
| B | GLU289 | |
| E | GLU289 | |
| F | GLU289 | |
| D | GLU289 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| 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 | ASP316 | |
| C | ASP316 | |
| B | ASP316 | |
| E | ASP316 | |
| F | ASP316 | |
| D | ASP316 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00318, ECO:0007744|PDB:6BFY, ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | LYS392 | |
| C | LYS392 | |
| B | LYS392 | |
| E | LYS392 | |
| F | LYS392 | |
| D | LYS392 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:30714720, ECO:0007744|PDB:6BFY |
| Chain | Residue | Details |
| A | SER41 | |
| C | SER41 | |
| B | SER41 | |
| E | SER41 | |
| F | SER41 | |
| D | SER41 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0007744|PDB:6BFY |
| Chain | Residue | Details |
| A | HIS158 | |
| F | GLU208 | |
| D | HIS158 | |
| D | GLU208 | |
| A | GLU208 | |
| C | HIS158 | |
| C | GLU208 | |
| B | HIS158 | |
| B | GLU208 | |
| E | HIS158 | |
| E | GLU208 | |
| F | HIS158 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0007744|PDB:6BFY, ECO:0007744|PDB:6BFZ |
| Chain | Residue | Details |
| A | GLU167 | |
| C | GLU167 | |
| B | GLU167 | |
| E | GLU167 | |
| F | GLU167 | |
| D | GLU167 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 18 |
| Details | SITE: Interaction with RNase E => ECO:0000269|PubMed:16516921, ECO:0000269|PubMed:20823555 |
| Chain | Residue | Details |
| A | LYS119 | |
| E | LYS119 | |
| E | GLU375 | |
| E | GLN407 | |
| F | LYS119 | |
| F | GLU375 | |
| F | GLN407 | |
| D | LYS119 | |
| D | GLU375 | |
| D | GLN407 | |
| A | GLU375 | |
| A | GLN407 | |
| C | LYS119 | |
| C | GLU375 | |
| C | GLN407 | |
| B | LYS119 | |
| B | GLU375 | |
| B | GLN407 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
| Chain | Residue | Details |
| A | LYS256 | |
| C | LYS256 | |
| B | LYS256 | |
| E | LYS256 | |
| F | LYS256 | |
| D | LYS256 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:31328167 |
| Chain | Residue | Details |
| A | LYS341 | |
| C | LYS341 | |
| B | LYS341 | |
| E | LYS341 | |
| F | LYS341 | |
| D | LYS341 |
