6NPF
Structure of E.coli enolase in complex with an analog of the natural product SF-2312 metabolite.
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 | 17 |
| Details | binding site for residue TLA A 601 |
| Chain | Residue |
| A | GLY39 |
| A | LYS341 |
| A | ARG370 |
| A | SER371 |
| A | LYS392 |
| A | MG603 |
| A | HOH701 |
| A | HOH706 |
| A | HOH712 |
| A | ALA40 |
| A | SER41 |
| A | GLN166 |
| A | GLU167 |
| A | ASP245 |
| A | GLU289 |
| A | ASP316 |
| A | LEU339 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 602 |
| Chain | Residue |
| A | LYS179 |
| A | GLU180 |
| A | ARG183 |
| B | ARG57 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 603 |
| Chain | Residue |
| A | ASP245 |
| A | GLU289 |
| A | ASP316 |
| A | TLA601 |
| A | HOH712 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 604 |
| Chain | Residue |
| A | ARG57 |
| B | LYS179 |
| B | GLU180 |
| B | ARG183 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue GOL A 605 |
| Chain | Residue |
| A | HOH702 |
| B | GOL503 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue TLA 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 | ARG370 |
| B | SER371 |
| B | LYS392 |
| B | MG502 |
| B | HOH605 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | ASP245 |
| B | GLU289 |
| B | ASP316 |
| B | TLA501 |
| B | HOH605 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| A | GOL605 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 B 504 |
| Chain | Residue |
| B | GLY-4 |
| B | ARG-3 |
| C | ARG-3 |
| D | ARG-3 |
| E | GLN-6 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 C 701 |
| Chain | Residue |
| C | LYS179 |
| C | GLU180 |
| C | ARG183 |
| D | ARG57 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 702 |
| Chain | Residue |
| C | ASP245 |
| C | GLU289 |
| C | ASP290 |
| C | ASP316 |
| C | TLA703 |
| C | HOH807 |
| site_id | AD3 |
| Number of Residues | 17 |
| Details | binding site for residue TLA C 703 |
| Chain | Residue |
| C | GLY39 |
| C | ALA40 |
| C | SER41 |
| C | HIS158 |
| C | GLN166 |
| C | GLU167 |
| C | ASP245 |
| C | GLU289 |
| C | ASP316 |
| C | LYS341 |
| C | ARG370 |
| C | SER371 |
| C | LYS392 |
| C | MG702 |
| C | HOH804 |
| C | HOH807 |
| C | HOH815 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 C 704 |
| Chain | Residue |
| C | LYS428 |
| C | GLY429 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue GOL C 705 |
| Chain | Residue |
| A | HOH743 |
| C | MET-5 |
| C | HOH823 |
| site_id | AD6 |
| Number of Residues | 16 |
| Details | binding site for residue KVM D 601 |
| Chain | Residue |
| D | ASP316 |
| D | LEU339 |
| D | LYS341 |
| D | HIS369 |
| D | ARG370 |
| D | SER371 |
| D | LYS392 |
| D | MG604 |
| D | GLY39 |
| D | ALA40 |
| D | SER41 |
| D | GLN166 |
| D | GLU167 |
| D | GLU208 |
| D | ASP245 |
| D | GLU289 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 D 602 |
| Chain | Residue |
| C | ARG57 |
| D | GLU180 |
| D | ARG183 |
| site_id | AD8 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 D 603 |
| Chain | Residue |
| A | GLN-6 |
| D | ARG-3 |
| D | GLY-4 |
| D | HOH702 |
| E | ARG-3 |
| F | ARG-3 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue MG D 604 |
| Chain | Residue |
| D | ASP245 |
| D | GLU289 |
| D | ASP316 |
| D | KVM601 |
| D | HOH711 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL D 605 |
| Chain | Residue |
| D | HOH705 |
| D | HOH713 |
| D | HOH724 |
| D | HOH727 |
| D | HOH731 |
| D | HOH742 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 D 606 |
| Chain | Residue |
| D | GLU21 |
| D | MET33 |
| D | ALA35 |
| D | GLU375 |
| D | ASP376 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 F 701 |
| Chain | Residue |
| E | ARG57 |
| F | LYS179 |
| F | GLU180 |
| F | ARG183 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue MG F 702 |
| Chain | Residue |
| F | ASP245 |
| F | GLU289 |
| F | ASP316 |
| F | KVM703 |
| F | HOH811 |
| site_id | AE5 |
| Number of Residues | 17 |
| Details | binding site for residue KVM F 703 |
| 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 | MG702 |
| F | HOH811 |
| site_id | AE6 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 F 704 |
| Chain | Residue |
| E | ARG183 |
| F | ARG57 |
| site_id | AE7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 F 705 |
| Chain | Residue |
| A | ARG-3 |
| B | ARG-3 |
| C | GLN-6 |
| F | GLY-4 |
| F | ARG-3 |
| site_id | AE8 |
| Number of Residues | 6 |
| Details | binding site for residue MG E 601 |
| Chain | Residue |
| E | ASP245 |
| E | GLU289 |
| E | ASP316 |
| E | LYS392 |
| E | KVM602 |
| E | HOH701 |
| site_id | AE9 |
| Number of Residues | 15 |
| Details | binding site for residue KVM E 602 |
| Chain | Residue |
| E | GLY39 |
| E | ALA40 |
| E | SER41 |
| E | GLN166 |
| E | GLU167 |
| E | GLU208 |
| E | ASP245 |
| E | ASP316 |
| E | LYS341 |
| E | ARG370 |
| E | SER371 |
| E | LYS392 |
| E | MG601 |
| E | HOH701 |
| E | HOH708 |
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 | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15003462","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15003462","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]} |
| 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":"11676541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16516921","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20823555","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H8A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11676541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20823555","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30714720","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H8A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11676541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16516921","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20823555","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 174 |
| Details | Region: {"description":"Interaction with RNase E"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"30714720","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 18 |
| Details | Site: {"description":"Interaction with RNase E","evidences":[{"source":"PubMed","id":"16516921","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20823555","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"31328167","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
