4ZA0
Structure of Human Enolase 2 in complex with Phosphonoacetohydroxamate
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 | 5 |
| Details | binding site for residue MG A 501 |
| Chain | Residue |
| A | ASP245 |
| A | GLU293 |
| A | ASP318 |
| A | PAH503 |
| A | HOH635 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | SER40 |
| A | PAH503 |
| A | HOH633 |
| A | HOH702 |
| site_id | AC3 |
| Number of Residues | 19 |
| Details | binding site for residue PAH A 503 |
| Chain | Residue |
| A | GLY38 |
| A | ALA39 |
| A | SER40 |
| A | GLN166 |
| A | GLU167 |
| A | ASP245 |
| A | GLU293 |
| A | ASP318 |
| A | LEU341 |
| A | LYS343 |
| A | ARG372 |
| A | SER373 |
| A | LYS394 |
| A | MG501 |
| A | MG502 |
| A | HOH633 |
| A | HOH641 |
| A | HOH702 |
| A | HOH706 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MG B 501 |
| Chain | Residue |
| B | ASP245 |
| B | GLU293 |
| B | ASP318 |
| B | PAH503 |
| B | HOH608 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | SER40 |
| B | PAH503 |
| B | HOH630 |
| B | HOH695 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | binding site for residue PAH B 503 |
| Chain | Residue |
| B | GLY38 |
| B | ALA39 |
| B | SER40 |
| B | GLN166 |
| B | GLU167 |
| B | ASP245 |
| B | GLU293 |
| B | ASP318 |
| B | LEU341 |
| B | LYS343 |
| B | ARG372 |
| B | SER373 |
| B | LYS394 |
| B | MG501 |
| B | MG502 |
| B | HOH630 |
| B | HOH670 |
| B | HOH695 |
| B | HOH790 |
Functional Information from PROSITE/UniProt
| site_id | PS00164 |
| Number of Residues | 14 |
| Details | ENOLASE Enolase signature. LLLKvNQIGSVTEA |
| Chain | Residue | Details |
| A | LEU340-ALA353 |
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 | GLU210 | |
| B | GLU210 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00924 |
| Chain | Residue | Details |
| A | LYS343 | |
| B | LYS343 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P06733 |
| Chain | Residue | Details |
| A | SER40 | |
| B | SER40 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P00924 |
| Chain | Residue | Details |
| A | HIS158 | |
| B | ASP318 | |
| B | SER370 | |
| B | LYS394 | |
| A | GLU167 | |
| A | GLU293 | |
| A | ASP318 | |
| A | SER370 | |
| A | LYS394 | |
| B | HIS158 | |
| B | GLU167 | |
| B | GLU293 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP245 | |
| B | ASP245 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P06733 |
| Chain | Residue | Details |
| A | SER2 | |
| B | SER2 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06733 |
| Chain | Residue | Details |
| A | LYS5 | |
| A | LYS64 | |
| A | LYS193 | |
| A | LYS256 | |
| B | LYS5 | |
| B | LYS64 | |
| B | LYS193 | |
| B | LYS256 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231 |
| Chain | Residue | Details |
| A | THR26 | |
| B | THR26 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
| Chain | Residue | Details |
| A | TYR44 | |
| B | TYR44 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182 |
| Chain | Residue | Details |
| A | LYS60 | |
| A | LYS89 | |
| A | LYS228 | |
| B | LYS60 | |
| B | LYS89 | |
| B | LYS228 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17183 |
| Chain | Residue | Details |
| A | LYS197 | |
| A | LYS199 | |
| B | LYS197 | |
| B | LYS199 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182 |
| Chain | Residue | Details |
| A | LYS202 | |
| B | LYS202 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733 |
| Chain | Residue | Details |
| A | LYS233 | |
| B | LYS233 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | SER263 | |
| B | SER263 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06733 |
| Chain | Residue | Details |
| A | TYR287 | |
| B | TYR287 |
| site_id | SWS_FT_FI16 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06733 |
| Chain | Residue | Details |
| A | SER291 | |
| B | SER291 |
| site_id | SWS_FT_FI17 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17182 |
| Chain | Residue | Details |
| A | LYS335 | |
| A | LYS343 | |
| A | LYS406 | |
| B | LYS335 | |
| B | LYS343 | |
| B | LYS406 |
| 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 | LYS202 | |
| B | LYS202 |
