2AKM
Fluoride Inhibition of Enolase: Crystal Structure of the Inhibitory Complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0001917 | cellular_component | photoreceptor inner segment |
| A | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0005938 | cellular_component | cell cortex |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0009410 | biological_process | response to xenobiotic stimulus |
| A | 0009986 | cellular_component | cell surface |
| A | 0016020 | cellular_component | membrane |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019899 | molecular_function | enzyme binding |
| A | 0030426 | cellular_component | growth cone |
| A | 0032355 | biological_process | response to estradiol |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043025 | cellular_component | neuronal cell body |
| A | 0043204 | cellular_component | perikaryon |
| A | 0044877 | molecular_function | protein-containing complex binding |
| A | 0045121 | cellular_component | membrane raft |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0061621 | biological_process | canonical glycolysis |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0097060 | cellular_component | synaptic membrane |
| B | 0000015 | cellular_component | phosphopyruvate hydratase complex |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0001917 | cellular_component | photoreceptor inner segment |
| B | 0004634 | molecular_function | phosphopyruvate hydratase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0005938 | cellular_component | cell cortex |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006096 | biological_process | glycolytic process |
| B | 0009410 | biological_process | response to xenobiotic stimulus |
| B | 0009986 | cellular_component | cell surface |
| B | 0016020 | cellular_component | membrane |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019899 | molecular_function | enzyme binding |
| B | 0030426 | cellular_component | growth cone |
| B | 0032355 | biological_process | response to estradiol |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043025 | cellular_component | neuronal cell body |
| B | 0043204 | cellular_component | perikaryon |
| B | 0044877 | molecular_function | protein-containing complex binding |
| B | 0045121 | cellular_component | membrane raft |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0061621 | biological_process | canonical glycolysis |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0097060 | cellular_component | synaptic membrane |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 440 |
| Chain | Residue |
| A | ASP244 |
| A | GLU292 |
| A | ASP317 |
| A | HOH461 |
| A | HOH462 |
| A | HOH463 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 441 |
| Chain | Residue |
| A | HOH461 |
| A | HOH464 |
| A | HOH465 |
| A | SER39 |
| A | LYS342 |
| A | PO4442 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 442 |
| Chain | Residue |
| A | GLY37 |
| A | ALA38 |
| A | SER39 |
| A | HIS157 |
| A | LYS342 |
| A | ARG371 |
| A | SER372 |
| A | MG441 |
| A | HOH465 |
| A | HOH490 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 440 |
| Chain | Residue |
| B | ASP244 |
| B | GLU292 |
| B | ASP317 |
| B | HOH444 |
| B | HOH445 |
| B | HOH446 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 442 |
| Chain | Residue |
| B | ALA38 |
| B | SER39 |
| B | LYS342 |
| B | HIS370 |
| B | ARG371 |
| B | SER372 |
| B | HOH444 |
| B | HOH445 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS A 460 |
| Chain | Residue |
| A | THR40 |
| A | GLY41 |
| A | ILE42 |
| A | SER248 |
| A | GLU249 |
| A | GLN297 |
| A | HOH568 |
Functional Information from PROSITE/UniProt
| site_id | PS00164 |
| Number of Residues | 14 |
| Details | ENOLASE Enolase signature. LLLKvNQIGSVTEA |
| Chain | Residue | Details |
| A | LEU339-ALA352 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P00924 |
| Chain | Residue | Details |
| A | GLY210 | |
| B | GLY210 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00924 |
| Chain | Residue | Details |
| A | VAL343 | |
| B | VAL343 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P06733 |
| Chain | Residue | Details |
| A | THR40 | |
| B | THR40 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00924 |
| Chain | Residue | Details |
| A | ALA158 | |
| B | ASP318 | |
| B | HIS370 | |
| B | THR394 | |
| A | PHE167 | |
| A | ASP293 | |
| A | ASP318 | |
| A | HIS370 | |
| A | THR394 | |
| B | ALA158 | |
| B | PHE167 | |
| B | ASP293 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | VAL245 | |
| B | VAL245 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P06733 |
| Chain | Residue | Details |
| A | ILE2 | |
| B | ILE2 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06733 |
| Chain | Residue | Details |
| A | ILE5 | |
| A | ALA64 | |
| A | GLY193 | |
| A | TYR256 | |
| B | ILE5 | |
| B | ALA64 | |
| B | GLY193 | |
| B | TYR256 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231 |
| Chain | Residue | Details |
| A | ALA26 | |
| B | ALA26 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
| Chain | Residue | Details |
| A | GLU44 | |
| B | GLU44 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 |
| Chain | Residue | Details |
| A | GLY60 | |
| A | LEU89 | |
| A | GLU228 | |
| B | GLY60 | |
| B | LEU89 | |
| B | GLU228 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17183 |
| Chain | Residue | Details |
| A | ASP197 | |
| A | TYR199 | |
| B | ASP197 | |
| B | TYR199 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 |
| Chain | Residue | Details |
| A | ASP202 | |
| B | ASP202 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733 |
| Chain | Residue | Details |
| A | ALA233 | |
| B | ALA233 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | PRO263 | |
| B | PRO263 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06733 |
| Chain | Residue | Details |
| A | PRO287 | |
| B | PRO287 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06733 |
| Chain | Residue | Details |
| A | ILE291 | |
| B | ILE291 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17182 |
| Chain | Residue | Details |
| A | ALA335 | |
| A | VAL343 | |
| A | TYR406 | |
| B | ALA335 | |
| B | VAL343 | |
| B | TYR406 |
| site_id | SWS_FT_FI18 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P06733 |
| Chain | Residue | Details |
| A | ASP202 | |
| B | ASP202 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | GLU209 | |
| A | GLU166 | |
| A | HIS370 | |
| A | LYS393 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| B | GLU209 | |
| B | GLU166 | |
| B | HIS370 | |
| B | LYS393 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | LYS342 | |
| A | GLU209 | |
| A | GLU166 | |
| A | HIS370 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| B | LYS342 | |
| B | GLU209 | |
| B | GLU166 | |
| B | HIS370 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | LYS342 | |
| A | HIS189 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| B | LYS342 | |
| B | HIS189 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| A | LYS342 | |
| A | VAL240 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1els |
| Chain | Residue | Details |
| B | LYS342 | |
| B | VAL240 |
